Thermodynamics of spontaneous protein folding: role of …

Summary

Free energy change in individual transformations

It is standard practice in biochemistry to consider the Gibbs Free Energy of transformation of the sort A B in isolation in determining whether it will proceed spontaneously. A chemical reaction for which G is negative may generate heat (i.e. have a negative enthalpy change (H) ) which affects its aqueous surroundings, but it seems justified to consider the reaction in isolation as there is no sense that the change in the vibration of the water molecules is driving or coupled to the reaction.

This approach has been applied to the structural change of protein folding with the conclusion (consistent with the first explanation) that the change in enthalpy (H) is sufficient to produce a negative G and hence drive protein folding (Citation 1, below).

Free energy change in coupled transformationsMany biochemical changes involve transformations which individually have a positive free energy change, but are made possible by coupling to another reaction with negative free energy change, of greater magnitude:

A B , G1 = +x

C D , G2 = y

If y>x and these two reactions are coupled (generally through a complex reaction path on an enzyme) , then we have:

A + C B + D , Goverall = ve

See also Berg et al.

Although one can reject the second explanation in the question as it stands because it ignores the free energy change in the protein folding, perhaps it was intended to mean that the folding of the protein (A B) should be considered as coupled to the change in the environment of the water (C D), and that the negative G for the aqueous environment made a greater contribution to the overall G than that for the protein folding.

Is it valid to consider these two systems as coupled? In the original version of my answer I argued against this point of view, but am no longer convinced by my own arguments. The water environment is clearly essential for the hydrophobic effect the burying of the hydrophobic residues in the centre of the protein away from the water. This is evident if one considers the same protein in a hydrophobic environment such as a cell membrane it would not fold. In membrane proteins it is hydrophobic residues that are exposed to the lipid bilayer and it is their interiors that sometimes have hydrophilic channels.

So in this coupled system, what is the determinant of the negative free energy change? Minikel (Citation 2, below) asserts that there is no net enthalpy change for the protein folding, and it is the entropy effect on the G for the aqueous environment that drives the folding. He indicates that this view is supported by differential scanning colorimetry and, although he doesnt cite references, there is a recent (if rather complex) review of this topic by Christopher M. Johnson.

Citation 1: Assertion of role of H of protein

The following explanation, taken from Essential Biochemistry, treats the protein folding in isolation and asserts that change in enthalpy is sufficient to produce a negative free energy change:

The folding of a protein also provides an example of the "H" and "TS" terms competing with one another to determine the G of the folding process. As described above, the change in entropy of the protein as it folds is negative, so the "TS" term is positive. However, in addition to entropic effects there are enthalpic contributions to protein folding. These include hydrogen bonding, ionic salt bridges, and Van der Waals forces. An input of thermal (heat) energy is required to disrupt these forces, and conversely when these interactions form during protein folding they release heat (the H is negative). When all of these entropic and enthalpic contributions are weighed, the enthalpy term wins out over the entropy term. Therefore the free energy of protein folding is negative, and protein folding is a spontaneous process.

Citation 2: Rebuttal of role of H of protein and assertion of role of water

The following explanation, taken from on-line lecture notes of of Eric V. Minikel of Harvard University, rebutting the point of view above:

An incorrect and simplistic view of protein folding is as follows. An unfolded protein has high configurational entropy but also high enthalpy because it has few stabilizing interactions. A folded protein has far less entropy, but also far less enthalpy. There is a tradeoff between H and S here. Note that because G = H - TS, increased temperature weights the S term more heavily, meaning that higher temperature favors unfolding.

That entire explanation only considers the energy of the protein and not that of the solvent. In fact, hydrophobic domains of a protein constrain the possible configurations of surrounding water (see explanation above), and so their burial upon folding increases the waters entropy. Moreover, it turns out that the hydrogen bonding of polar residues and the backbone is satisfied both in an unfolded state (by water) and in a folded state (by each other). Therefore enthalpy is zero sum, and protein folding is driven almost entirely by entropy.

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Thermodynamics of spontaneous protein folding: role of ...

Molecular Biology 02: ‘Thermodynamics of protein folding’

These are my notes from lecture 02 of Harvards BCMP 200: Molecular Biology course, delivered by Joe Loparo on September 5, 2014.

Continued from lecture 01. is always 0 or +180. If you plot and you find only a few clusters are well-represented: a range of -helix combinations, a -sheet area, and a third rarer area (called L and populated by left-handed -helices). is ususally found in the trans conformation due to steric hindrance of the consecutive side chains, however, proline because it is anchored to the backbone has a unique twist that enables a cis conformation.

-helices and -sheets are two ways of allowing the NH and C=O groups on the backbone to form hydrogen bonds. -helices contain 3.6 residues per rotation, or in other words, each residue spans 100 of rotation. Consecutive rungs of an -helix turns are separated by 5.4. -helices are almost exclusively right-handed. In a right-handed -helix, you turn counter-clockwise as you go up. In a left-handed -helix you turn clockwise as you go up. Side chains point outward from the helix. If you plot out where each residue falls on the helix based on the 3.6 residues/turn rule, you find that amphipathic, half-buried helices have all the hydrophobic residues on one side and the hydrophilic ones on the other side. A fully buried helix will be all hydrophobic residues and a fully exposed helix will be all hydrophilic residues.

In -sheets, all potential H-bonds are satisfied except for the flanking strands at either end of the sheet. About 20% of -sheets found in nature are mixed parallel and anti-parallel, the other 80% are pure one or the other. -sheets are not flat, but pleated.

A single sheet or helix is not stable in water. Tertiary structure is the packing of these elements, and loops connecting them, onto each other.

There are two fundamental problems in protein folding:

As an example, consider the metalloprotease cleaveage of Notch to create the Notch intracellular domain (NICD), which then translocates to the nucleus and affects transcription. The proteolytic site of Notch is protected by Lin12/Notch repeats which are connected to the EGF repeats that interact with Notchs ligand. The ligand is believed to apply a force that unfolds this region, allowing cleavage. Mutations which destabilize this fold and result in constitutive activation cause tumors.

Thermodynamics can only describe whether a chemical reaction will occur spontaneously or not, not how fast it will occur (see Biochemistry 01).

The energy of a system is its capacity to do work.

U = q + w

Where U is internal energy, q is heat and w is work.

q := heat = C(Tf-Ti)

Where C is the heat capacity and f and i mean final and initial.

w := work = Fxx

Where F is force and x is displacement along the x axis.

If you dissolve urea in water at a 4M solution, it will dissolve spontaneously and the solution will become cold (just like guanidine, as I learned here).

Gibbs free energy is defined as:

G = H - TS

Where G, H, T and S are Gibbs free energy, enthalpy, temperature and entropy respectively.

G = H - TS

If G < 0 the reaction will proceed spontaneously.

In the urea example, H > 0 because energy is required to pull apart the interacting urea molecules, using heat from the water. Yet the reaction still occurs spontaneously because S > 0 by a lot - the urea solution is much more entropic than urea and water separately.

For the reaction A + B C + D, we define:

Keq = ([C]eq[D]eq)/([A]eq[B]eq)

Keq = e-G/RT

ATP is a special molecule: its hydrolysis into ADP is spontaneous at physiological concentrations of the reactants and products, i.e. G < 0 for this reaction:

ATP + H2O ADP + Pi

Le Chateliers principle says you could drive the reaction in reverse, making ATP spontaneously, simply by increasing the concentrations of the procuts. However [Pi] never gets high enough in the cell for ATP to be spontaneously generated from ADP. The unfavorable production of ATP is instead created via a coupled reaction with favorable reactions such as the release of protons across the mitochondrial membrane (see Biochemistry 08).

H := Enthalpy = U + PV

Where U, P and V are internal energy, pressure and volume.

In physiological conditions, changes in pressure and volume are almost always negligible, so H and U are closely coupled. In other words, in most biological systems, the enthalpy is equal to the internal energy.

People have developed molecular dynamics simulations of the fundamental atomic forces that determine a proteins enthalpy (dihedral angles, Van der Waals interactions, electrostatic interactions, etc) and attempt to minimize the energy to determine a proteins fold. But there are so many degrees of freedom that computational expense prohibits running the simulation long enough to find the lowest energy state. Still there are attempts, such as Folding@Home, Foldit, and D.E. Shaws Anton. Anton holds the record for the longest molecular dynamics simulation - it ran for some untold amount of time, calculating the energy a protein would have at every femtosecond or something, in order to simulate 1 millisecond of the proteins movement. Obviously, the time that Anton took to simulate that millisecond was more than a millisecond.

S := Entropy = kbln(W)

Where kb is Boltzmanns constant and W is the number of microstates that give rise to the macrostate of interest.

My favorite explanation of this is that given by Richard Feynman. When I read it, I understood for the first time how physical entropy and information entropy are the same concept:

So we now have to talk about what we mean by disorder and what we mean by order. Suppose we divide the space into little volume elements. If we have black and white molecules, how many ways could we distribute them among the volume elements so that white is on one side and black is on the other? On the other hand, how many ways could we distribute them with no restriction on which goes where? Clearly, there are many more ways to arrange them in the latter case. We measure disorder by the number of ways that the insides can be arranged, so that from the outside it looks the same. The logarithm of that number of ways is the entropy. The number of ways in the separated case is less, so the entropy is less, or the disorder is less.

Richard Feynman, quoted here

In biology, entropy is very often the driving force, for instance for the burial of hydrophobic protein domains. Imagine a water molecule in a tetrahedron. The tetrahedron has four corners, and the water has two hydrogens, so you can place the molecule in 4 choose 2 = 6 orientations. If you add a nonpolar group of a neighboring molecule at one corner of the tetrahedron, only three of the six states remain favorable (by still allowing hydrogen bonding). So Shydrophobic = kbln(3) - kbln(6) < 0, meaning that entropy has decreased.

Consider the mixing of epoxy and hardener into cured epoxy. This reaction has S < 0 because the solid has fewer microstates than the liquids did. Yet the reaction occurs spontaneously at room temperature, so it must be true that H < 0. Heat is therefore released - in fact, the reaction is extremely exothermic. Joe measured the temperature of 5-minute epoxy and it rose from 21C to >40C at the 5 minute mark.

An incorrect and simplistic view of protein folding is as follows. An unfolded protein has high configurational entropy but also high enthalpy because it has few stabilizing interactions. A folded protein has far less entropy, but also far less enthalpy. There is a tradeoff between H and S here. Note that because G = H - TS, increased temperature weights the S term more heavily, meaning that higher temperature favors unfolding.

That entire explanation only considers the energy of the protein and not that of the solvent. In fact, hydrophobic domains of a protein constrain the possible configurations of surrounding water (see explanation above), and so their burial upon folding increases the waters entropy. Moreover, it turns out that the hydrogen bonding of polar residues and the backbone is satisfied both in an unfolded state (by water) and in a folded state (by each other). Therefore enthalpy is zero sum, and protein folding is driven almost entirely by entropy.

Here is a description of a technique called differential scanning calorimetry. You apply equal amounts of heat to two solutions, one with only buffer and the other with buffer and protein, and you measure the temperature in each solution. Eventually the protein reaches its melting temperature Tm, where the protein is 50% folded and 50% unfolded and G = 0. At Tm, the melting of the protein aborbs lots of the applied heat, and so the temperature does not rise as much as it does in the buffer-only solution.

Another technique for measuring protein stability is the force required to unfold it using single molecule atomic force microscopy.

Common denaturants are urea and guanidine hydrochloride. Amazingly, we still do not know how they work. It is thought that they stabilize all constituent parts of the unfolded protein. Guanidine may surround those unfavorable hydrophobic domains of the protein but then expose its own hydrophilic side to water, so that the movement of the water is not constrained.

Continued here:

Molecular Biology 02: 'Thermodynamics of protein folding'

The Science Behind Foldit | Foldit

Foldit is a revolutionary crowdsourcing computer game enabling you to contribute to important scientific research. This page describes the science behind Foldit and how your playing can help.

What is a protein? Proteins are the workhorses in every cell of every living thing. Your body is made up of trillions of cells, of all different kinds: muscle cells, brain cells, blood cells, and more. Inside those cells, proteins are allowing your body to do what it does: break down food to power your muscles, send signals through your brain that control the body, and transport nutrients through your blood. Proteins come in thousands of different varieties, but they all have a lot in common. For instance, they're made of the same stuff: every protein consists of a long chain of joined-together amino acids.

What are amino acids? Amino acids are small molecules made up of atoms of carbon, oxygen, nitrogen, sulfur, and hydrogen. To make a protein, the amino acids are joined in an unbranched chain, like a line of people holding hands. Just as the line of people has their legs and feet "hanging" off the chain, each amino acid has a small group of atoms (called a sidechain) sticking off the main chain (backbone) that connects them all together. There are 20 different kinds of amino acids, which differ from one another based on what atoms are in their sidechains. These 20 amino acids fall into different groups based on their chemical properties: acidic or alkaline, hydrophilic (water-loving) or hydrophobic (greasy).

What shape will a protein fold into? Even though proteins are just a long chain of amino acids, they don't like to stay stretched out in a straight line. The protein folds up to make a compact blob, but as it does, it keeps some amino acids near the center of the blob, and others outside; and it keeps some pairs of amino acids close together and others far apart. Every kind of protein folds up into a very specific shape -- the same shape every time. Most proteins do this all by themselves, although some need extra help to fold into the right shape. The unique shape of a particular protein is the most stable state it can adopt. Picture a ball at the top of a hill -- the ball will always roll down to the bottom. If you try to put the ball back on top it will still roll down to the bottom of the hill because that is where it is most stable.

Why is shape important? This structure specifies the function of the protein. For example, a protein that breaks down glucose so the cell can use the energy stored in the sugar will have a shape that recognizes the glucose and binds to it (like a lock and key) and chemically reactive amino acids that will react with the glucose and break it down to release the energy.

What do proteins do? Proteins are involved in almost all of the processes going on inside your body: they break down food to power your muscles, send signals through your brain that control the body, and transport nutrients through your blood. Many proteins act as enzymes, meaning they catalyze (speed up) chemical reactions that wouldn't take place otherwise. But other proteins power muscle contractions, or act as chemical messages inside the body, or hundreds of other things. Here's a small sample of what proteins do:

Proteins are present in all living things, even plants, bacteria, and viruses. Some organisms have proteins that give them their special characteristics:

You can find more information on the rules of protein folding in our FAQ.

What big problems is this game tackling?

How does my game playing contribute to curing diseases?

With all the things proteins do to keep our bodies functioning and healthy, they can be involved in disease in many different ways. The more we know about how certain proteins fold, the better new proteins we can design to combat the disease-related proteins and cure the diseases. Below, we list three diseases that represent different ways that proteins can be involved in disease.

What other good stuff am I contributing to by playing?

Proteins are found in all living things, including plants. Certain types of plants are grown and converted to biofuel, but the conversion process is not as fast and efficient as it could be. A critical step in turning plants into fuel is breaking down the plant material, which is currently done by microbial enzymes (proteins) called "cellulases". Perhaps we can find new proteins to do it better.

Can humans really help computers fold proteins?

Were collecting data to find out if humans' pattern-recognition and puzzle-solving abilities make them more efficient than existing computer programs at pattern-folding tasks. If this turns out to be true, we can then teach human strategies to computers and fold proteins faster than ever!

You can find more information about the goals of the project in our FAQ.

Brian Koepnick, Jeff Flatten, Tamir Husain, Alex Ford, Daniel-Adriano Silva, Matthew J. Bick, Aaron Bauer, Gaohua Liu, Yojiro Ishida, Alexander Boykov, Roger D. Estep, Susan Kleinfelter, Toke Nrgrd-Solano, Linda Wei, Foldit Players, Gaetano T. Montelione, Frank DiMaio, Zoran Popovi, Firas Khatib, Seth Cooper and David Baker. De novo protein design by citizen scientists Nature (2019). [link]

Thomas Muender, Sadaab Ali Gulani, Lauren Westendorf, Clarissa Verish, Rainer Malaka, Orit Shaer and Seth Cooper.Comparison of mouse and multi-touch for protein structure manipulation in a citizen science game interface.Journal of Science Communication (2019). [link]

Lorna Dsilva, Shubhi Mittal, Brian Koepnick, Jeff Flatten, Seth Cooper and Scott Horowitz.Creating custom Foldit puzzles for teaching biochemistry.Biochemistry and Molecular Biology Education (2019). [link]

Seth Cooper, Amy L. R. Sterling, Robert Kleffner, William M. Silversmith and Justin B. Siegel.Repurposing citizen science games as software tools for professional scientists.Proceedings of the 13th International Conference on the Foundations of Digital Games (2018). [link]

Robert Kleffner, Jeff Flatten, Andrew Leaver-Fay, David Baker, Justin B. Siegel, Firas Khatib and Seth Cooper. Foldit Standalone: a video game-derived protein structure manipulation interface using Rosetta. Bioinformatics (2017). [link]

Jacqueline Gaston and Seth Cooper. To three or not to three: improving human computation game onboarding with a three-star system. Proceedings of the SIGCHI Conference on Human Factors in Computing Systems (2017). [link]

Scott Horowitz, Brian Koepnick, Raoul Martin, Agnes Tymieniecki, Amanda A. Winburn, Seth Cooper, Jeff Flatten, David S. Rogawski, Nicole M. Koropatkin, Tsinatkeab T. Hailu, Neha Jain, Philipp Koldewey, Logan S. Ahlstrom, Matthew R. Chapman, Andrew P. Sikkema, Meredith A. Skiba, Finn P. Maloney, Felix R. M. Beinlich, Foldit Players, University of Michigan students, Zoran Popovi, David Baker, Firas Khatib and James C. A. Bardwell. Determining crystal structures through crowdsourcing and coursework. Nature Communications 7, Article number: 12549 (2016). [link]

Dun-Yu Hsiao, Min Sun, Christy Ballweber, Seth Cooper and Zoran Popovi. Proactive sensing for improving hand pose estimation. Proceedings of the SIGCHI Conference on Human Factors in Computing Systems (2016). [link]

Dun-Yu Hsiao, Seth Cooper, Christy Ballweber and Zoran Popovi. User behavior transformation through dynamic input mappings. Proceedings of the 9th International Conference on the Foundations of Digital Games (2014). [link]

George A. Khoury, Adam Liwo, Firas Khatib, Hongyi Zhou, Gaurav Chopra, Jaume Bacardit, Leandro O. Bortot, Rodrigo A. Faccioli, Xin Deng, Yi He, Pawel Krupa, Jilong Li, Magdalena A. Mozolewska, Adam K. Sieradzan, James Smadbeck, Tomasz Wirecki, Seth Cooper, Jeff Flatten, Kefan Xu, David Baker, Jianlin Cheng, Alexandre C. B. Delbem, Christodoulos A. Floudas, Chen Keasar, Michael Levitt, Zoran Popovi, Harold A. Scheraga, Jeffrey Skolnick, Silvia N. Crivelli and Foldit Players. WeFold: a coopetition for protein structure prediction. Proteins (2014). [link]

Christopher B. Eiben, Justin B. Siegel, Jacob B. Bale, Seth Cooper, Firas Khatib, Betty W. Shen, Foldit Players, Barry L. Stoddard, Zoran Popovi and David Baker. Increased Diels-Alderase activity through backbone remodeling guided by Foldit players. Nature Biotechnology (2012). [link]

Erik Andersen, Eleanor O'Rourke, Yun-En Liu, Richard Snider, Jeff Lowdermilk, David Truong, Seth Cooper and Zoran Popovi. The impact of tutorials on games of varying complexity. Proceedings of the SIGCHI Conference on Human Factors in Computing Systems (2012). [link]

Firas Khatib, Seth Cooper, Michael D. Tyka, Kefan Xu, Ilya Makedon, Zoran Popovi, David Baker and Foldit Players. Algorithm discovery by protein folding game players. Proceedings of the National Academy of Sciences of the United States of America (2011). [link]

Miroslaw Gilski, Maciej Kazmierczyk, Szymon Krzywda, Helena Zbransk, Seth Cooper, Zoran Popovi, Firas Khatib, Frank DiMaio, James Thompson, David Baker, Iva Pichov and Mariusz Jaskolskia. High-resolution structure of a retroviral protease folded as a monomer. Acta Crystallographica (2011). [link]

Firas Khatib, Frank DiMaio, Foldit Contenders Group, Foldit Void Crushers Group, Seth Cooper, Maciej Kazmierczyk, Miroslaw Gilski, Szymon Krzywda, Helena Zbransk, Iva Pichov, James Thompson, Zoran Popovi, Mariusz Jaskolski and David Baker. Crystal structure of a monomeric retroviral protease solved by protein folding game players. Nature Structural and Molecular Biology (2011). [link]

Seth Cooper, Firas Khatib, Ilya Makedon, Hao Lu, Janos Barbero, David Baker, James Fogarty, Zoran Popovi and Foldit Players. Analysis of social gameplay macros in the Foldit cookbook. Proceedings of the 6th International Conference on the Foundations of Digital Games (2011). [link]

Seth Cooper, Firas Khatib, Adrien Treuille, Janos Barbero, Jeehyung Lee, Michael Beenen, Andrew Leaver-Fay, David Baker, Zoran Popovi and Foldit Players. Predicting protein structures with a multiplayer online game. Nature (2010). [link]

Seth Cooper, Adrien Treuille, Janos Barbero, Andrew Leaver-Fay, Kathleen Tuite, Firas Khatib, Alex Cho Snyder, Michael Beenen, David Salesin, David Baker, Zoran Popovi and Foldit players. The challenge of designing scientific discovery games. Proceedings of the 5th International Conference on the Foundations of Digital Games (2010). [link]

Foldit has been in dozens of publications over the years - to list them all would take a page of their own. For a sampling, please see our Center for Game Science page.

Check out the Rosetta@Home Screensaver to see how computers fold proteins using distributed computing.

Thank you for using Foldit in your classroom! We have put together a set of instructions to assist you in setting up your students to play Foldit.

You can find the researchers and supporters associated with this study on the game's credits page.

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The Science Behind Foldit | Foldit

Early Results of Human Trials For Anti-Aging Drug Are …

David Sinclair of Harvard University has been working toward a molecular fountain of youth. Finding previous success in mice, early human trials have begun in small studies around the globe. Preliminary results of these studies indicate that the treatments are safe and do not induce major adverse side effects, but it is still far too early to tell if the treatments will actually be effective at reversing aging in humans.

A normal part of human aging involves senescence, which is a general wearing out of the body over time. Muscles begin to lose tone and become inflamed over time, and they also can develop insulin resistance. Without being able to use insulin, the cells arent able to uptake the glucose needed for activity. These problems contribute to why many elderly people have trouble getting around and athletes arent able to sustain certain levels of activity as they age.

Last December, Sinclairs group published a paper in Cell revealing that they had been able to drastically reduce the functional age of muscle tissue. Treating the mice with the metabolic co-enzyme NAD+ effectively reversed the aging process within the skeletal muscle by increasing muscle tone and producing effects similar to eating a healthy diet and exercising.

Over time, NAD+ levels decrease, which limits the cells ability to produce ATP in the mitochondria for energy. As the mice grew older and less active, their levels of NAD+ had basically been cut in half. By replenishing this critical compound in the mice, their muscles had been rejuvenated. The natural process that deteriorates skeletal muscle is the same one that affects the heart.

If the relative effects that were seen in the mice could be replicated in humans, it would result in a 60-year-old with the physique of a 20-year-old. The human studies that began this year following a period of financial uncertainty are initially only auditing the treatments safety, by taking stock of all side effects that could occur and identify negative interactions with other medications. The first studies have been fairly small, but will continue to grow.

Results from human studies that explore the treatments efficacy will not appear for a few more years, though Sinclair is optimistic. He told ABC that this treatment has the potential to allow individuals to lead long, healthy lives. He described the potential of his anti-aging therapy to one day be regarded similarly and ubiquitously as antibiotics.

"Some people say it's like playing God, but if you ask somebody 100 years ago, what about antibiotics? They probably would have said the same thing," he told ABCs Sue Lannin. "Some people worry about big advances in technology and medicine, but once it's adapted and it's natural for people to live until they're 90 in a healthy way ... we'll look back at today like we do at the times before antibiotics when people died from an infected splinter."

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Early Results of Human Trials For Anti-Aging Drug Are ...

Low T Specialist – Dallas, TX & Frisco, TX: Men’s T-Clinic …

What causes Low T?

Men may notice the effects of lower testosterone production after age 30. Additionally, Low T can be the result of primary testicular failure or a problem that originates in the testicles. Another cause of Low T happens in the pituitary gland the part of the brain that signals the testicles to produce testosterone. Low T can also occur as the result of an injury or infection.

Other factors that contribute to Low T may include:

Low T can present a variety of symptoms. Some of them mirror the symptoms of other medical problems as well, so its important not to ignore them. Seek treatment from a mens health care specialist if you have any of the following for more than a few days at a time.

The regulation and production of testosterone is the responsibility of the hypothalamus and pituitary gland. The body balances hormone levels when its functioning properly. For men with Low T, the body is either not signaling production effectively or it is not able to produce effective levels once it is given the signal to do so.

With testosterone injections, the hypothalamus and pituitary gland respond by signaling the testes to decrease natural production. Men who discontinue therapy revert back to their pre-therapy baseline testosterone levels. If those levels have been diagnosed as being inadequate, stopping the injections means you return to experiencing the symptoms you had before beginning treatment.

The only way to monitor your testosterone level effectively and identify potential issues is with multiple blood tests. This helps your doctor identify the proper dose specifically for you. No one likes to give blood, but the trained staff members at Mens T-Clinic make the process as painless as possible.

Testosterone production levels can vary, and a single blood test is just a snapshot of your bodys current production. Multiple factors can determine your level at any given time. For example, increases in the cortisol hormone (which increases with stress) have been known to lower testosterone.

Testosterone levels from 350 ng/mL to 1000 ng/mL are considered normal, but you could be in the low to normal range and experience symptoms.

Your doctor diagnoses hypogonadism by considering symptoms and testosterone levels. If you are borderline and have symptoms, you may qualify for therapy. Call or schedule an appointment online to learn about your options.

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Low T Specialist - Dallas, TX & Frisco, TX: Men's T-Clinic ...

Nanomedicine Conferences 2019 | Nanotechnology Meetings …

Pharmaceutical Nanotechnology & Nanomedicine Congress 2020

LexisConferencesconsider it a privilege and a matter of great pride to host Conference on Pharmaceutical Nanotechnology & Nanomedicine Congressis to be held at Venice, Italyfor the duration of May 11-12, 2020. On this auspicious occasion, Organizing Committee invites the participants from all over the world to take part in this annual flagship conference with the theme Exploring the Progress of Nanomedicinewith Trending Nanotechnologies. The conference will provide a forum for interaction among attendees on Pharmaceutical Nanotechnology, Development of Nanotechnology-enabled Devices, Micro Fluidics platform for Nano Particle Synthesis, Toxicology and Risk Assessment of Nanomedicine Systems, MedicalNano Devices and Biosensors, Synthesis of Nanoparticles for Drug Delivery, Nanomedicine for Immune System and Cancer Diagnosis & Therapy.

This global meeting will assemble the world leaders in the expanding fields related to Pharmaceutical Nanotechnology & Nanomedicine. It will create an interface among professionals, academic faculty members, Researchers, Nanotech representatives and students, Nanotechnologists, Manufacturing Medical Device and experts in the fields of Nanotechnology. industry practitioners.The Conference will also have a room for companies and/or institutions to present their services, products, revolutions and research results.

Global Market for Nanotechnology products was priced $22.9 billion in 2013 and unanticipated increased to about $26 billion in 2014. This market is await to reach about $64.2 billion by 2019; a compound annual growth rate (CAGR) is 19.8% from 2014 to 2019. The global market for nanotechnology-enabled printing technology was approximate to be at total $14 billion in 2013. The market is anticipate to grow at a compound annual growth rate (CAGR) of 17.7% over the next five years and to total $31.8 billion by 2018.

Details of Nanomedicine Congress 2020

Conference Name

Place

Date

Nanomedicine Congress 2020

Venice, Italy

May 11-12, 2020

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Nanomedicine Conferences 2019 | Nanotechnology Meetings ...

Aesthetic Medicine & Anti-Aging Clinic | Baton Rouge …

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We also sell many beneficial skin care products so you can maintain your vibrant, healthy appearance in the comfort of your home. Call today to learn more about our beautifying spa services, skin care products and anti-aging treatments in Baton Rouge and Lafayette, LA and schedule your free consultation.

Botox and Vaser liposuction will make you look great, but if you have a hormone imbalance, you likely wont feel as good as you look. If you are suffering from lower energy and libido, increased weight gain and other seemingly unexplainable issues, it may be due to a hormone imbalance. We specialize in hormone replacement therapy, including testosterone replacement. Call today to schedule your free consultation with a hormone replacement therapist and discover if hormone replacement therapy is the solution to the issues that affect your quality of life.

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Aesthetic Medicine & Anti-Aging Clinic | Baton Rouge ...

What Is Transhumanism? – thecut.com

Photo: Rick Friedman/Corbis via Getty Images

A recent New York Times story revealed that Jeffrey Epstein, alleged sex trafficker and megarich financier, has long held beliefs in transhumanism, defined by the Times as the science of improving the human population through technologies like genetic engineering and artificial intelligence. But what does that mean, and what would it entail?

What does Jeffrey Epstein have to do with transhumanism?

For his part, Epstein hoped to spread his DNA throughout the human race by impregnating women at his New Mexico ranch presumably under the assumption that his DNA is somehow superior to the average humans. Epstein was able to attract a number of prominent scientist friends, including George M. Church, a Harvard professor and geneticist who has done work on synthetic genes, and evolutionary biologist Stephen Jay Gould (now deceased).

According to the Times, Epstein was able to lure scientists into his circle through lavish spending, both personally and professionally, in the form of research donations. The Times story suggests that Epsteins money encouraged some scientists to lend credence to Epsteins transhumanist ideals, though others insist they remained critical. (Harvard cognitive psychologist Steven Pinker called him an intellectual impostor.)

Where did Epstein get these ideas?

According to the Times, the scientist and author Jaron Lanier said that a NASA scientist he once met at one of Epsteins dinner parties told Lanier that Epstein had been inspired by the story of the Repository for Germinal Choice, an elitist sperm bank created in 1980 with the express goal of strengthening the human gene pool with the sperm of Nobel Prize winners. Though 200 babies were eventually born of the banks efforts, none were the offspring of actual Nobel winners, and the repository shut down in 1999. Mr. Lanier said that he had the impression that Epstein used his exclusive dinner parties as a way to screen female guests for their potential to bear Epsteins children.

Are there other transhumanists out there?

Apparently.In 2011, one of Epsteins charities gave $20,000 to an organization then called the Worldwide Transhumanist Association. Now rebranded as Humanity Plus, the website defines transhumanism as the desire for people to be better than well. Humanity Plus is primarily an educational organization, hosting conferences and leadership summits on topics related to transhumanism. Their site includes a page dedicated to the Transhumanist Declaration, which includes the statement: We believe that humanitys potential is still mostly unrealized. There are possible scenarios that lead to wonderful and exceedingly worthwhile enhanced human conditions.

Epsteins foundation (now defunct) also paid $100,000 salary to Humanity Pluss vice chairman, Ben Goertzel.

What does transhumanism have to do with eugenics?

Critics of transhumanism have compared the philosophy to eugenics, the discredited and ill-used belief that controlled breeding could improve the human race. Alan M. Dershowitz, a professor emeritus of law at Harvard, told the Times that conversations Epstein initiated with him called to mind the Nazis use of eugenics as justification for genocide. (Dershowitz, nonetheless, represented Epstein in court preceding his 2008 conviction on charges of soliciting prostitution from a minor.)

The difference between transhumanism and eugenics, then, is that transhumanism does not explicitly encourage controlled human breeding, nor the propagation of a particular race. Still, both movements envision a superior human race, a goal which (history indicates) is inseparable from sociocultural ideals and prejudices.

Does the field of transhumanism have any scientific credibility?

There is certainly interest: A recent study published in Nature Nanotechnology examined the potential for intersection between humans and machines, according to one of its authors, Dr. Yunlong Zhao from the Advanced Technology Institute at the University of Surrey.

Anqi Zhang, another of the studys authors, told The Independent he expects significant advancement in the next 10 to 15 years in the transhumanist field specifically, the interface between man and machine, as recently depicted on the BBC show Years and Years.

At present, though, the technology required to complete such a transhumanist goal does not exist, which, as The Week reports, has encouraged some scientists to pursue cryogenic preservation, or freezing their bodies until such technology exists. (Cryogenic preservation is, itself, a scientifically dubious endeavor.)

An unnamed transhumanist told the Times that Epstein had told him he wanted his head and his penis to be cryogenically frozen.

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Protein Folding – an overview | ScienceDirect Topics

8 INHIBITORS OF HEAT-SHOCK PROTEINS (HSP 90)

Protein folding is catalysed in vivo by isomerases and chaperone proteins. Molecular chaperones are ubiquitous proteins that assist folding, assembly, transport, and degradation of proteins within the cell. The first identified chaperones were heat-shock proteins (HSPs), whose names is derived from the elevated levels produced when cells are grown at higher-than-normal temperatures. HSPs stabilize other proteins during their synthesis and assist in protein folding by binding and releasing unfolded or misfolded proteins using an ATP-independent mechanism. Proteins unable to maintain their proper shape are broken down by the proteasome (see Section 1 of Chapter 10) and eliminated, as shown in Fig. 9.33. These events may be favourable if the proteins are previously mutated and hence dangerous for the survival of the cell, but they become a problem if the proteins are necessary for its normal functioning.

Figure 9.33. Function of heat-shock proteins.

HSP 90 is the best known of HSPs and its activity is coupled to an ATPase cycle that is controlled by several cofactors. It has three major domains, namely a highly conserved N-terminal ATPase domain, a middle domain, and a C-terminal dimerization domain. The crystal structure of HSP 90 bound to ATP has shown how this nucleotide is hydrolysed,135 but the detailed mechanism of protein folding remains unknown.

HSP 90 has emerged as an attractive cancer target because its inhibition blocks a large number of cancer-related signalling pathways since a large number of intra-cellular signalling molecules require association with HSP 90 to achieve their active conformation, correct cellular location, and stability.136 These include steroid hormone receptors, transcription factors like the tumor suppressor protein p53 and kinases like Src-kinase.

The conformational changes that take place in HSP 90 after binding and hydrolysis of ATP regulate the stabilization and maturation of client proteins, including hypoxia-inducible factor-1 (HIF-1), a relevant anticancer target.137 This ATP site is known by X-ray crystallography to be very different from that of kinases, allowing the design of inhibitors with high selectivity with regard to other ATP-binding proteins.

The design and study of selective inhibitors of HSP 90 was initially controversial because this protein is critical for the survival of both normal and sick cells. However, HSP does not have much activity under normal conditions. When the cell is under stress by genetic mutations or environmental changes such as heat or infection HSP 90 activity is increased as an emergency response that stabilizes partially unfolded proteins and helps them to achieve their correct shape. This activity also assists the survival of cancer cells despite an abundance of misfolded and unstable proteins, and this is one of the reasons to study HSP 90 as an anticancer target.

The main strategy employed in the design of HSP 90 inhibitors is based in the synthesis of analogues of the natural antitumor geldanamycin, a benzoquinone derivative belonging to the ansamycin class, although some companies working in this field are designing entirely synthetic molecules not related to this compound.

Geldanamycin was originally believed to be a TK inhibitor, but it was later identified as an ATP-competitive inhibitor of HSP 90. It could not be advanced to the clinical stage because it showed unacceptable hepatotoxicity, probably associated with the presence of the electrophilic methoxybenzoquinone moiety. For this reason, displacement of the 17-methoxy group by nucleophiles led to less toxic analogues such as tanespimycin (17-allylaminogeldanamycin, 17-AAG).138 Another problem associated with geldanamycin is its very low solubility, which was solved with the development of the water-soluble analogue alvespimycin (17-dimethylaminoethylaminogeldanamycin, 17-DMAG).139 Both analogues were better tolerated than the parent natural product and are under clinical trials. In another approach, the problematic quinone moiety of 17-AAG was reduced to the hydroquinone stage. The resulting compound, IPI-504, can be formulated as a soluble salt that is suitable for intravenous or oral formulations. It has shown encouraging results in Phase I trials in patients with gastrointestinal stromal tumors that were resistant to imatinib, although further clinical development is necessary.

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Protein Folding - an overview | ScienceDirect Topics

Longevity claims – Wikipedia

This article is about modern, or complete, unvalidated supercentenarian claims up to the age of 130 years. For validated specific supercentenarian claims by modern standards, see List of the verified oldest people. For historical, incomplete claims, including all claims over 130 years, see Longevity myths.

Longevity claims are unsubstantiated cases of asserted human longevity. Those asserting lifespans of 110 years or more are referred to as supercentenarians. Many have either no official verification or are backed only by partial evidence. Cases where longevity has been fully verified, according to modern standards of longevity research, are reflected in an established list of supercentenarians based on the work of organizations such as the Gerontology Research Group (GRG) or Guinness World Records. This article lists living claims greater than that of the oldest person whose age has been independently verified, Kane Tanaka at 116years, 274days, and deceased claims greater than that of the oldest person ever whose age has been verified, namely Jeanne Calment who died at the age of 122 years, 164 days. The upper limit for both lists is 130 years.

Prior to the 19th century, there was insufficient evidence either to demonstrate or to refute centenarian longevity.[1] Even today, no fixed theoretical limit to human longevity is apparent.[2] Studies[1] in the biodemography of human longevity indicate a late-life mortality deceleration law: that death rates level off at advanced ages to a late-life mortality plateau. This implies that there is no fixed upper limit to human longevity, or fixed maximum human lifespan.[3]Researchers in Denmark have found a way to determine when a person was born using radiocarbon dating done on the lens of the eye.[4]

In 1955, Guinness World Records began maintaining a list of the verified oldest people.[5] It developed into a list of all supercentenarians whose lifespan had been verified by at least three documents, in a standardized process, according to the norms of modern longevity research. Many unverified cases ("claims" or "traditions") have been controverted by reliable sources. Taking reliable demographic data into account, these unverified cases vary widely in their plausibility.

In numerous editions from the 1960s through the 1980s, Guinness stated that

No single subject is more obscured by vanity, deceit, falsehood, and deliberate fraud than the extremes of human longevity.[7]

Despite demographic evidence of the known extremes of modern longevity, stories in otherwise reliable sources still surface regularly, stating that these extremes have been exceeded. Responsible, modern, scientific validation of human longevity requires investigation of records following an individual from birth to the present (or to death); purported longevity far outside the demonstrated records regularly fail such scrutiny.

Actuary Walter G. Bowerman stated that ill-founded longevity assertions originate mainly in remote, underdeveloped regions, among non-literate peoples, with only family testimony available as evidence.[8] This means that people living in areas of the world with historically more comprehensive resources for record-keeping have tended to hold more claims to longevity, regardless of whether or not individuals in other parts of the world have lived longer.

In the transitional period of record-keeping, records tend to exist for the wealthy and upper-middle classes, but are often spotty and nonexistent for the middle classes and the poor. In the United States, birth registration did not begin in Mississippi until 1912 and was not universal until 1933. Hence, in many longevity cases, no actual birth record exists. This type of case is classified by gerontologists as "partially validated".[citation needed]

Since some cases were recorded in a census or in other reliable sources, obtainable evidence may complete full verification.

In another type of case, the only records that exist are late-life documents. Because age inflation often occurs in adulthood (to avoid military service or to apply for a pension early), or because the government may have begun record-keeping during an individual's lifetime, cases unverified by proximate records exist. These unverified cases are less likely to be true (because the records are written later), but are still possible. Longevity narratives were not subjected to rigorous scrutiny until the work of William Thoms in 1873. Thoms proposed the 100th-birthday test: is there evidence to support an individual's claimed age at what would be their centenary birthday?[10][11] This test does not prove a person's age, but does winnow out typical pension-claim longevity exaggerations and spontaneous claims that a certain relative is over 150.

These are standardized lists of people whose lifespans remain unverified by proximate records, including both modern (Guinness-era) and historical cases. All cases in which an individual's supercentenarian lifespan is not (yet) backed by records sufficient to the standards of modern longevity research are listed as unverified. They may be factually true, even though records do not exist (or have not yet been found), so such lists include these grey-area cases.

These living supercentenarian cases, in descending order of claimed age, with full birth and review dates, have been updated within the past two years, but have not had their claimed age validated by an independent body such as the Gerontology Research Group or Guinness World Records. Only claims greater than the oldest verified living person, Kane Tanaka, who is aged 116years, 274days, but under 130 years are included in the list.

This table contains supercentenarian claims with either a known death date or no confirmation for more than 2 years that they were still alive. Only claims greater than that of Jeanne Calment who died at the age of 122 years, 164 days, but under 130 years are included. They are listed in order of age as of the date of death or date last reported alive.

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Longevity claims - Wikipedia

Low Testosterone Therapy (TRT) and Treatment from Low T Center

Testosterone is a natural hormone responsible for the normal growth and development of the male sex organs and for maintenance of other sexual characteristics. In men, testosterone is produced in the testes (the reproductive glands that also produce sperm) and regulated by the hypothalamus and pituitary gland. With low levels of testosterone, men can experience a decrease in energy and libido, increase in body fat, and emotional changes.

A decrease in testosterone levels is to be expected as men age. Other factors can also contribute to low T, including chronic health issues such as diabetes or obesity, medications such as corticosteroids or trauma. Our comprehensive health assessment tests for low testosteronelevels as well as a multitude of other related issues and can be treated with customized, testosterone replacement therapy healthcare plans.

Its hard to pin down an exact number for exactly how common testosterone deficiency is among men. The condition becomes drastically more common as men age, and its estimated that as many as 40% of older men have low testosterone.

Many men, especially younger men, are nervous to seek treatment for low testosterone. While symptoms differ from person to person, men with low testosterone also experience a decrease in sex drive,erectile dysfunction, and heart disease. Waiting to seek help can lead to the late detection and worsening of these progressive conditions.

Low testosterone can result in a lack of energy. If you find that youre feeling sleepy for much of the day, even after youve had a good night of rest, theres a high chance that a hormonal imbalance is to blame. Many patients find that their energy levels soar after they begin testosterone therapy.

Testosterone encourages muscle growth. When men do not have enough testosterone, it can inhibit muscle growth. Muscle tissue burns calories at a higher rate than fat tissue. When men have low testosterone, it can result in fat gain, and for mostmen, that gain happens around the belly and hips. Sometimes, the imbalance of testosterone and estrogen can cause men to hold onto more body fat than they would otherwise.

Studies have shown that men who take testosterone tend to experience an increase in memory. Testosterone affects many physical processes in the body, and focus, clarity, and memory are no exception. Life issues caused by low testosterone- such as sexual and relationship issues- can also play a role in the struggle to focus.

While most men experience a decrease in sex drive as they age, low testosterone causes a steeper drop-off than what is normal for most men. Low testosterone can cause a variety of health issues (such as hair loss and erectile dysfunction) that may also inhibit sexual desire.

Low testosterone can result in a number of mood changes. Hormonal imbalances are often to blame for depression, anxiety, and other mood issues. Fatigue caused by low testosterone can also add to these issues.

Since testosterone is key for building muscle in the body, low testosterone can cause loss of muscle mass. This loss of mass can also add to fat gain, as previously mentioned.

Some men begin to lose hair as they age, andlow testosterone can also play a role, especially if the balding occurs suddenly.

See All Symptoms

By knowing your testosterone numbers, our medical professionals can provide quality treatment for low T and other underlying conditions. Your path to vitality happens with four steps:

By treating the symptoms of low testosterone, patients feel energized, stronger, and less irritable; enjoy more productive sleep and a renewed sense of self; find it easier to concentrate and remember; and experience an increase in libido.

Because Low T Center takes a holistic approach to mens healthcare, our medical professionals can proactively address other conditions youre currently experiencing or could experience later on, includingsleep apneaorallergies.These conditions may also affect testosterone levels.

Our providers get to know you on a personal level and gather important health data often to assess progress with greater efficiency.

At Low T Center, we focus on treating your symptoms of low testosterone levels, so you can rediscover the best version of yourself.

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What 6 World Religions Have To Say About Vegetarianism

No, this is not a sermon. You have no excuse to fall asleep.

Vegetarianism has a strong tradition in Judaism, as the original design for the Garden of Eden. In an early chapter of Genesis it is written that, I give you every seed-bearing plant that is upon the earth, and every tree that has seed-bearing fruit; they shall be yours for food." The Book of Daniel is also viewed as a bedrock of religious support for vegetarianism. When the prophet Daniel and three fellow slaves were in captivity, they were offered the Kings rich diet but refused and asked for only vegetables to eat, and water to drink. This verse has led to both a 10-day cleansing program and the highly successful lifestyle change program at the Saddleback Church in southern California.

Jewish dietary law stresses avoidance of cruelty to animals, whether in the production of food or as beasts of burden. More can be learned about the rich culture of green Judaism at http://www.jewishveg.com. Out of interest, I wanted to find out if there are organizations promoting vegetarian diets in other world religions.

Christianity: Amongst the many branches of Christianity, the strongest teachings come within the Seventh-day Adventist Church. Founder Ellen White was vegetarian, and lacto-ovo-vegetarianism is officially promoted. Research on followers of this religion has been helpful in demonstrating better health and lifespan in those adhering to plant-based diets. There are groups of scholars that maintain Jesus was a vegetarian.

Islam: Vegetarianism among Muslims is an active movement stressing kindness, mercy and compassion for animals. The mainstream of Muslims who eat meat often follow laws called halal, which allow clean animals that are properly slaughtered. Certain animals are not permitted, depending on how they are killed, and pork is also forbidden.

Hinduism: There is a strong tradition of vegetarianism in the Hindu religions, stemming from the Krishna cult and the reverence for the sacred cow. Vegetarianism is viewed as a daily sadhana or spiritual practice by many Hindus.

Buddhism: There is a strong tradition of vegetarianism in Buddhism and Mahayah monks are strict followers as well as many lay followers.

Jainism: Originating about the same time as the Hindu and Buddhist religions, Jainism stresses the practice of ahimsa or non violence. Jains believe in abstaining from meat and honey, and harming any living creature even insects is avoided.

Lessons of mercy to animals and respect for the planet found in many of the world religions are just one of the many paths that may lead you to choose a plant-based diet. In our open society, where the cruelty and excess of concentrated animal feeding operations has been well documented in several popular movies, ahimsa takes on new urgency. Whatever basis forms your path towards whole food and plant-based meals, you will share a strong tradition with many ethically concerned individuals. In the words of Albert Einstein, Nothing will benefit human health and increase the chances for survival of life on earth as much as the evolution to a vegetarian diet.

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What 6 World Religions Have To Say About Vegetarianism

Protein Structures: Primary, Secondary, Tertiary, Quaternary …

Proteins are the largest and most varied class of biological molecules, and they show the greatest variety of structures. Many have intricate three-dimensional folding patterns that result in a compact form, but others do not fold up at all (natively unstructured proteins) and exist in random conformations. The function of proteins depends on their structure, and defining the structure of individual proteins is a large part of modern Biochemistry and Molecular Biology.

To understand how proteins fold, we will start with the basics of structure, and progress through to structures of increasing complexity.

Peptide Bonds

To make a protein, amino acids are connected together by a type of amide bond called a peptide bond. This bond is formed between the alpha amino group of one amino acid and the carboxyl group of another in a condensation reaction. When two amino acids join, the result is called a dipeptide, three gives a tripeptide, etc. Multiple amino acids result in a polypeptide (often shortened to peptide). Because water is lost in the course of creating the peptide bond, individual amino acids are referred to as amino acid residues once they are incorporated. Another property of peptides is polarity: the two ends are different. One end has a free amino group (called the N-terminal) and the other has a free carboxyl group (C-terminal).

In the natural course of making a protein, polypeptides are elongated by the addition of amino acids to the C-terminal end of the growing chain. Conventionally, peptides are written N-terminal first; therefore gly-ser is not the same as ser-gly or GS is not the same as SG. The connection gives rise to a repeating pattern of NCC-NCC-NCC atoms along the length of the molecule. This is referred to as the backbone of the peptide. If stretched out, the side chains of the individual residues project outwards from this backbone.

The peptide bond is written as a single bond, but it actually has some characteristics of a double bond because of the resonance between the C-O and C-N bonds:

This means that the six atoms involved are coplanar, and that there is not free rotation around the CN axis. This constrains the flexibility of the chain and prevents some folding patterns.

Primary Structure of Proteins

It is convenient to discuss protein structure in terms of four levels (primary to quaternary) of increasing complexity. Primary structure is simply the sequence of residues making up the protein. Thus primary structure involves only the covalent bonds linking residues together.

The minimum size of a protein is defined as about 50 residues; smaller chains are referred to simply as peptides. So the primary structure of a small protein would consist of a sequence of 50 or so residues. Even such small proteins contain hundreds of atoms and have molecular weights of over 5000 Daltons (Da). There is no theoretical maximum size, but the largest protein so far discovered has about 30,000 residues. Since the average molecular weight of a residue is about 110 Da, that single chain has a molecular weight of over 3 million Daltons.

Secondary Structure

This level of structure describes the local folding pattern of the polypeptide backbone and is stabilized by hydrogen bonds between N-H and C=O groups. Various types of secondary structure have been discovered, but by far the most common are the orderly repeating forms known as the a helix and the b sheet.

An a helix, as the name implies, is a helical arrangement of a single polypeptide chain, like a coiled spring. In this conformation, the carbonyl and N-H groups are oriented parallel to the axis. Each carbonyl is linked by a hydrogen bond to the N-H of a residue located 4 residues further on in the sequence within the same chain. All C=O and N-H groups are involved in hydrogen bonds, making a fairly rigid cylinder. The alpha helix has precise dimensions: 3.6 residues per turn, 0.54 nm per turn. The side chains project outward and contact any solvent, producing a structure something like a bottle brush or a round hair brush. An example of a protein with many a helical structures is the keratin that makes up human hair.

The structure of a b sheet is very different from the structure of an a helix. In a b sheet, the polypeptide chain folds back on itself so that polypeptide strands like side by side, and are held together by hydrogen bonds, forming a very rigid structure. Again, the polypeptide N-H and C=O groups form hydrogen bonds to stabilize the structure, but unlike the a helix, these bonds are formed between neighbouring polypeptide (b) strands. Generally the primary structure folds back on itself in either a parallel or antiparallel arrangement, producing a parallel or antiparallel b sheet. In this arrangement, side chains project alternately upward and downward from the sheet. The major constituent of silk (silk fibroin) consists mainly of layers of b sheet stacked on top of each another.

Other types of secondary structure. While the a helix and b sheet are by far the most common types of structure, many others are possible. These include various loops, helices and irregular conformations. A single polypeptide chain may have different regions that take on different secondary structures. In fact, many proteins have a mixture of a helices, b sheets, and other types of folding patterns to form various overall shapes.

What determines whether a particular part of a sequence will fold into one or the other of these structures? A major determinant is the interactions between side chains of the residues in the polypeptide. Several factors come into play: steric hindrance between nearby large side chains, charge repulsion between nearby similarly-charged side chains, and the presence of proline. Proline contains a ring that constrains bond angles so that it will not fit exactly into an a helix or b sheet. Further, there is no H on one peptide bond when proline is present, so a hydrogen bond cannot form. Another major factor is the presence of other chemical groups that interact with each other. This contributes to the next level of protein structure, the tertiary structure.

Tertiary Structure

This level of structure describes how regions of secondary structure fold together that is, the 3D arrangement of a polypeptide chain, including a helices, b sheets, and any other loops and folds. Tertiary structure results from interactions between side chains, or between side chains and the polypeptide backbone, which are often distant in sequence. Every protein has a particular pattern of folding and these can be quite complex.

Whereas secondary structure is stabilized by H-bonding, all four weak forces contribute to tertiary structure. Usually, the most important force is hydrophobic interaction (or hydrophobic bonds). Polypeptide chains generally contain both hydrophobic and hydrophilic residues. Much like detergent micelles, proteins are most stable when their hydrophobic parts are buried, while hydrophilic parts are on the surface, exposed to water. Thus, more hydrophobic residues such as trp are often surrounded by other parts of the protein, excluding water, while charged residues such as asp are more often on the surface.

Other forces that contribute to tertiary structure are ionic bonds between side chains, hydrogen bonds, and van der Waals forces. These bonds are far weaker than covalent bonds, and it takes multiple interactions to stabilize a structure.

There is one covalent bond that is also involved in tertiary structure, and that is the disulfide bond that can form between cysteine residues. This bond is important only in non-cytoplasmic proteins since there are enzyme systems present in the cytoplasm to remove disulfide bonds.

Visualization of protein structures Because the 3D structures of proteins involve thousands of atoms in complex arrangements, various ways of depicting them so they are understood visually have been developed, each emphasizing a different property of the protein. Software tools have been written to depict proteins in many different ways, and have become essential to understanding protein structure and function.

Structural Domains of Proteins

Protein structure can also be described by a level of organization that is distinct from the ones we have just discussed. This organizational unit is the protein domain, and the concept of domains is extremely important for understanding tertiary structure. A domain is a distinct region (sequence of amino acids) of a protein, while a structural domain is an independently-folded part of a protein that folds into a stable structure. A protein may have many domains, or consist only of a single domain. Larger proteins generally consist of connected structural domains. Domains are often separated by a loosely folded region and may create clefts between them..

Quaternary Structure

Some proteins are composed of more than one polypeptide chain. In such proteins, quaternary structure refers to the number and arrangement of the individual polypeptide chains. Each polypeptide is referred to as a subunit of the protein. The same forces and bonds that create tertiary structure also hold subunits together in a stable complex to form the complete protein.

Individual chains may be identical, somewhat similar, or totally different. As examples, CAP protein is a dimer with two identical subunits, whereas hemoglobin is a tetramer containing two pairs of non-identical (but similar) subunits. It has 2 a subunits and 2 b subunits. Secreted proteins often have subunits that are held together by disulfide bonds. Examples include tetrameric antibody molecules that commonly have two larger subunits and two smaller subunits (heavy chains and light chains) connected by disulfide bonds and noncovalent forces.

In some proteins, intertwined a helices hold subunits together; these are called coiled-coils. This structure is stabilized by a hydrophobic surface on each a helix that is created by a heptameric repeat pattern of hydrophilic/hydrophobic residues. The sequence of the protein can be represented as abcdefgabcdefgabcdefg with positions a and d filled with hydrophobic residues such as A, V, L etc. Each a helix has a hydrophobic surface that therefore matches the other. When the two helices coil around each other, those surfaces come together, burying the hydrophobic side chains and forming a stable structure. An example of such a protein is myosin, the motor protein found in muscle that allows contraction.

Protein Folding

How and why do proteins naturally form secondary, tertiary and quaternary structures? This question is a very active area of research and is certainly not completely understood. A folded, biologically-active protein is considered to be in its native state, which is generally thought to be the conformation with least free energy.

Proteins can be unfolded or denatured by treatment with solvents that disrupt weak bonds. Thus organic solvents that disrupt hydrophobic interactions, high concentrations of urea or guanidine that interfere with H-bonding, extreme pH or even high temperatures, will all cause proteins to unfold. Denatured proteins have a random, flexible conformation and usually lack biological activity. Because of exposed hydrophobic groups, they often aggregate and precipitate. This is what happens when you fry an egg.

If the denaturing condition is removed, some proteins will re-fold and regain activity. This process is called renaturation. Therefore, all the information necessary for folding is present in the primary structure (sequence) of the protein. During renaturation, the polypeptide chain is thought to fold up into a loose globule by hydrophobic effects, after which small regions of secondary structure form into especially favorable sequences. These sequences then interact with each other to stabilize intermediate structures before the final conformation is attained.

Many proteins have great difficulty renaturing, and proteins that assist other proteins to fold are called molecular chaperones. They are thought to act by reversibly masking exposed hydrophobic regions to prevent aggregation during the multi-step folding process. Proteins that must cross membranes (eg. mitochondrial proteins) must stay unfolded until they reach their destination, and molecular chaperones may protect and assist during this process.

Protein families/Types of proteins

Proteins are classified in a number of ways, according to structure, function, location and/or properties. For example, many proteins combine tightly with other substances such as carbohydrates (glycoproteins), lipids (lipoproteins), or metal ions (metalloproteins). The diversity of proteins that form from the 20 amino acids is greatly increased by associations such as these. Proteins that are tightly bound to membranes are called membrane proteins. Proteins with similar activities are given functional classifications. For example, proteins that break down other proteins are called proteases.

Because almost all proteins arise by an evolutionary process, ie. new ones are derived from old ones, they can be classified into families by their relatedness. Proteins that derive from the same ancestor are called homologous proteins. Studying the sequences of homologous proteins can give clues to the structure and function of the protein. Residues that are critical for function do not change on an evolutionary timescale; they are referred to as conserved residues. Identifying such residues by comparing amino acid sequences often helps clarify what a protein is doing or how it is folded. For example the proteases trypsin and chymotrypsin are members of the serine protease family; so-named because of a conserved serine residue that is essential to catalyze the reaction. Trypsin and chymotrypsin contain very similar folding patterns and reaction mechanisms. Recognizing a pattern of conserved residues in protein sequences often allows scientists to deduce the function of a protein.

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Protein Structures: Primary, Secondary, Tertiary, Quaternary ...

Protein Folding – Anfinsen’s Experiment ~ Biology Exams 4 U

How Protein folds? During translation, the linear chain of amino acids formed will be gradually released from the ribosome, and these amino acids should fold properly to make a functional protein, the ultimate nano machines in the cells. Protein folding is undoubtedly the most critical events that determine the ability of that given protein to work properly.

How protein folds? Is it a random process? It shouldnt be, as folding determines the function.

Definition:

Protein folding refers to the set of ordered pathways by which protein folds into their native functional confirmation.

Protein folding is primarily driven by hydrophobic forces.

Anfinsen's Experiment

First step..

The first insight to this question was provided by Christian Anfinsen at the NIH. He was working on the properties of ribonuclease A (a single chain protein of 124 amino acids with 4 di-sulphide bonds). He unfolded (denatured) ribonuclease A using urea and mercaptoethanol (denaturants). The protein lost its function. Then he allowed to renature ribonuclease A by removing denaturants, and found out that ribonuclease A folded spontaneously and become functional. He concluded that Ribonuclease A can self assemble into its 3D functional structure.

Protein Folding inside the Cell

Inside the cell, protein folding is assisted by different proteins collectively called as accessory proteins.

The importance of studying protein folding?

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Protein Folding - Anfinsen's Experiment ~ Biology Exams 4 U

Denaturation and Protein Folding | Introduction to Chemistry

Each protein has its own unique sequence of amino acids and the interactions between these amino acids create a specify shape. This shape determines the proteins function, from digesting protein in the stomach to carrying oxygen in the blood.

If the protein is subject to changes in temperature, pH, or exposure to chemicals, the internal interactions between the proteins amino acids can be altered, which in turn may alter the shape of the protein. Although the amino acid sequence (also known as the proteins primary structure) does not change, the proteins shape may change so much that it becomes dysfunctional, in which case the protein is considered denatured. Pepsin, the enzyme that breaks down protein in the stomach, only operates at a very low pH. At higher pHs pepsins conformation, the way its polypeptide chain is folded up in three dimensions, begins to change. The stomach maintains a very low pH to ensure that pepsin continues to digest protein and does not denature.

Because almost all biochemical reactions require enzymes, and because almost all enzymes only work optimally within relatively narrow temperature and pH ranges, many homeostatic mechanisms regulate appropriate temperatures and pH so that the enzymes can maintain the shape of their active site.

It is often possible to reverse denaturation because the primary structure of the polypeptide, the covalent bonds holding the amino acids in their correct sequence, is intact. Once the denaturing agent is removed, the original interactions between amino acids return the protein to its original conformation and it can resume its function.

However, denaturation can be irreversible in extreme situations, like frying an egg. The heat from a pan denatures the albumin protein in the liquid egg white and it becomes insoluble. The protein in meat also denatures and becomes firm when cooked.

Chaperone proteins (or chaperonins) are helper proteins that provide favorable conditions for protein folding to take place. The chaperonins clump around the forming protein and prevent other polypeptide chains from aggregating. Once the target protein folds, the chaperonins disassociate.

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Denaturation and Protein Folding | Introduction to Chemistry

56 Delicious Vegetarianism Facts | FactRetriever.com

1Andrews, Ryan.Drop The Fat Act and Live Lean. Summertown, TN: Healthy Living Publication.2012.

2Cox, Peter. You Dont Need Meat. New York, NY: Thomas Dunne Books, 2002.

3Foer, Jonathan Safran. Eating Animals. New York, NY: Little, Brown, and Company, 2009.

4Freston, Kathy. "A Vegan Diet (Hugely) Helpful Against Cancer." The Huffington Post. December 9, 2012. Updated: February 8, 2013. Accessed: August 25, 2016.

5Hellmich, Nanci. USDA: Eggs Cholesterol Level Better Than Cracked Up to Be. USA Today. February 8, 2011. Accessed: February 23, 2013.

6MacRae, Fiona. Real Men Must Eat Meat, Say Women as They Turn up Their Noses at Vegetarians. Daily Mail. February 1, 2011. Accessed: February 17, 2013.

7Nelson, Dean. India Tells West to Stop Eating Beef. The Telegraph. November 20, 2009. Accessed: February 17, 2013.

8Pamer, Melissa. Meatless Mondays: LA Urges Residents to Turn Vegetarian One Day a Week. U.S. News. November 10, 2012. Accessed: November 26, 2012.

9Plant-based Protein Sources. SoyStache. 2012. Accessed: November 26, 2012.

10Robbins, John. Diet for a New America. Tiburon, CA: Stillpoint Publishing, 1987.

11Saunders, Kerrie K. The Vegan Diet as Chronic Disease Prevention. New York, NY: Lantern Books, 2003.

12Spencer, Colin.Vegetarianism: A History. New York, NY: Four Walls Eight Windows, 2000.

13Stuart, Tristram.The Bloodless Revolution: A Cultural History of Vegetarianism from 1600 to Modern Times. New York, NY: W. W. Norton & Company, 2006.

14The Number of Vegetarians in the World. Raw Food Health. Accessed: February 23, 2013.

15Wanjek, Christopher. Sorry Vegans, Eating Meat and Cooking Food Is How Humans Got Their Big Brains. The Washington Post. November 26, 2012. Accessed: February 17, 2013.

16Williams, Amanda. Vegetarians Have a Better Sex Life: Eating Tofu Can Boost You in the Bedroom, New Study Claims. Daily Mail. November 23, 2012. Accessed: February 17, 2013.

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56 Delicious Vegetarianism Facts | FactRetriever.com

Twenty-Two Reasons Not to Go Vegetarian

Currently making the rounds on the internet is an article resurrected from a 1999 issue of Vegetarian Times, 22 Reasons to Go Vegetarian.

Consider making this healthy choice as one of your new years resolutions. . . says the teaser. Stacks of studies confirm that a diet full of fresh fruits and vegetables and grains is your best bet for living a longer, healthier and more enjoyable life. There are literally hundreds of great reasons to switch to a plant-based diet; here are 22 of the best.

Leaving aside for the moment the fact that a plant-based diet is not necessarily the same as a vegan diet, and that in the US a diet containing fresh fruits, vegetables and whole grains is a marker for prosperity and health consciousness (and therefore would naturally give better results than a diet lacking in these items), lets look first at the American origins of the premise that a diet composed largely of fruits, vegetables and grains (presumably whole grains) is a passport to good health.

The American Vegetarian Society was founded in 1850 by Sylvester Graham (1794- 1851), an early advocate of dietary reform in United States and the inventor of Graham bread, made from chemical-free unsifted flour. Highly influential, Graham promoted vegetarianism and a high-fiber diet as a cure for alcoholism and lust. Graham preached that an unhealthy diet (one containing the confounding variables of meat and white flour) stimulated excessive sexual desire, which irritated the body and caused disease.

John Harvey Kellogg (1852-1943) followed in Grahams footsteps. Inventor of corn flakes and a process for making peanut butter, Kellogg advocated a high-fiber vegetarian diet to combat the twin evils of constipation and natural urges. Kellogg preached against sexual activity even in marriage.

Today we recognize the demonization and suppression of natural urges as a recipe for the pathological expression thereof; in fact wed probably label Graham and Kellogg as nut cases suffering from serious insecurities. But the diet proposed to accomplish their goal of character building and social piety is still with us, enshrined, in fact, in the government-sanctioned food pyramid based on grains, vegetables and fruits with the addition of small amounts of lowfat animal foods. Lop off the top of the pyramid and you have the vegan diet, still promoted with religious fervor even though its original dogmatic basis has been forgotten. The language of moral rectitude still lurks in the vegetarian arguments of sexually liberated New Age youth.

With these paradoxes in mind, lets examine the 22 reasons given for adopting a vegan diet.

Vegetarians live about seven years longer, and vegans (who eat no animal products) about 15 years longer than meat eaters, according to a study from Loma Linda University. These findings are backed up by the China Health Project (the largest population study on diet and health to date), which found that Chinese people who eat the least amount of fat and animal products have the lowest risks of cancer, heart attack and other chronic degenerative diseases.

Reference please? We havent found such statistics in a search of the medical database.

In spite of claims to stacks of studies, there is actually very little scientific literature that carefully compares mortality and disease rates in vegetarians and nonvegetarians. In 1991, Dr. Russell Smith, a statistician, analyzed the existing studies on vegetariansim1 and discovered that while a number of studies show that vegetarian diets significantly decrease blood cholesterol levels, very few have evaluated the effects of vegetarian diets on overall mortality. His careful analysis (see sidebar below) revealed no benefit from vegetarianism in terms of overall mortality or longevity. In fact, Smith speculated on the possibility that the available data from the many existing prospective studies were left unpublished because they failed to reveal any benefits of the vegetarian diet. He notes, for example, mortality statistics are strangely absent from the Tromso Heart Study in Norway, which showed that vegetarians had slightly lower blood cholesterol levels than nonvegetarians.2

Since the publication of Russell Smiths analysis, two significant reports on vegetarianism and mortality have appeared in the literature. One was a 2005 German paper that compared mortality in German vegetarians and health-conscious persons in a 21-year followup.7 By comparing vegetarians with health-conscious meat eaters, the German researchers eliminated the major problem in studies that claim to have found better mortality rates in vegetarians compared to the general population. Vegetarians tend not to smoke, drink alcohol or indulge in sugar and highly processed foods. To compare these individuals to meat-eaters on the typical western diet will naturally yield results that favor vegetarianism. But in the German study, both vegetarians and nonvegetarian health-conscious persons had reduced mortality compared with the general population, and it was other factorslow prevalence of smoking and moderate or high levels of physical activitythat were associated with reduced overall mortality, not the vegetarian diet.

The other was a 2003 report that followed up on The Health Food Shoppers Study in the 1970s and the Oxford Vegetarians Study in the 1980s.8 The mortality of both the vegetarians and the nonvegetarians in these studies was low compared with national rates in the UK. Within the studies, mortality for major causes of death was not significantly different between vegetarians and nonvegetarians, although there was a non-significant reduction in mortality from ischemic heart disease among vegetarians.

As for Colin Campbells China Study, often cited as proof that plant-based diets are healthier than those containing animal foods, the data on consumption and disease patterns collected by the Cornell University researchers in their massive dietary survey do not support such claims. What the researchers discovered was that meat eaters had lower triglycerides and less cirrhosis of the liver, but otherwise they found no strong correlation, either negative or positive, with meat eating and any disease.9

In his introduction to the research results, study director Campbell refers to considerable contemporary evidence supporting the hypothesis that the lowest risk for cancer is generated by the consumption of a variety of fresh plant products.10 Yet Cornell researchers found that the consumption of green vegetables, which ranged from almost 700 grams per day to zero, depending on the region, showed no correlation, either positive or negative, with any disease. Dietary fiber intake seemed to protect against esophageal cancer, but was positively correlated with higher levels of TB, neurological disorders and nasal cancer. Fiber intake did not confer any significant protection against heart disease or most cancers, including cancer of the bowel.

In a 1999 article published in Spectrum, Campbell claimed the Cornell findings suggested that a diet high in animal products produces disease, and a diet high in grains, vegetables and other plant matter produces health.11 Such statements by the now-famous Campbell are misleading, to put it mildly, and have influenced many unsuspecting consumers to adopt a vegetarian lifestyle in the hopes of improving their health.

Cardiovascular disease is still the number one killer in the United States, and the standard American diet (SAD) thats laden with saturated fat and cholesterol from meat and dairy is largely to blame. Plus, produce contains no saturated fat or cholesterol. Incidentally, cholesterol levels for vegetarians are 14 percent lower than meat eaters

Stacks of evidence now exist to refute the notion that cholesterol levels and consumption of saturated fat have anything to do with heart disease, but this is a convenient theory for promoting vegetable oil consumption at the expense of animal fats. The International Atherosclerosis Project found that vegetarians had just as much atherosclerosis as meat eaters.12 Vegetarians also have higher levels of homocysteine, a risk marker for heart disease.13

The standard American diet is not, unfortunately, laden with saturated fat and cholesterol. It is, however, laden with trans fats and refined vegetable oils, both derived from plants, and it is these processed fats and oils that are associated with the increase in heart disease, not saturated animal fats.

Replacing meat, chicken and fish with vegetables and fruits is estimated to cut food bills.

Some plant foods, such as nuts and breakfast cereals, are very expensive. And any analysis of your food budget must necessarily include medical and dental expenses, and also account for reduced income due to missed days at work, lack of energy and the behavioral difficulties that result from B12 deficiency. A lowcost vegetarian diet that renders you incapable of performing a well-paid, high-stress jobthe kind that allows you to put money into a mutual fundis a poor bargain in the long-term.

Studies done at the German Cancer Research Center in Heidelberg suggest that this is because vegetarians immune systems are more effective in killing off tumour cells than meat eaters. Studies have also found a plant-based diet helps protect against prostate, colon and skin cancers.

The claim that vegetarians have lower rates of cancer compared to nonvegetarians has been squarely contradicted by a 1994 study comparing vegetarians with the general population.14 Researchers found that although vegetarian Seventh Day Adventists have the same or slightly lower cancer rates for some sites, for example 91 percent instead of 100 percent for breast cancer, the rates for numerous other cancers are much higher than the general US population standard, especially cancers of the reproductive tract. SDA females had more Hodgkins disease (131 percent), more brain cancer (118 percent), more malignant melanoma (171 percent), more uterine cancer (191 percent), more cervical cancer (180 percent) and more ovarian cancer (129 percent) on average.

According to scientists at the Cancer Research UK Epidemiology Unit, University of Oxford, Studies of cancer have not shown clear differences in cancer rates between vegetarians and non vegetarians.15

Meat, chicken and fish tend to come in boring shades of brown and beige, but fruits and vegetables come in all colors of the rainbow. Disease fighting phytochemicals are responsible for giving produce their rich, varied hues. So cooking by color is a good way to ensure youre eating a variety of naturally occurring substances that boost immunity and prevent a range of illnesses

Salmon, eggs and butter have beautiful color. Nothing prevents meat-eaters from adding color to their plate by using a variety of vegetables and fruits. The nutrients from these plant foods will be more easily absorbed if you serve them with butter or cream. Animal foods provide an abundance of naturally occurring substances that boost immunity and prevent a range of illnesses.

On average, vegetarians are slimmer than meat eaters, and when we diet, we keep the weight off up to seven years longer. Thats because diets that are higher in vegetable proteins are much lower in fat and calories than the SAD. Vegetarians are also less likely to fall victim to weight-related disorders like heart disease, stroke and diabetes

Studies do show that vegetarians on average have lower body mass than non-vegetarians, but vegetarianism does not confer protection from stroke and diabetes and provides only minimal protection against heart disease. Some people do gain weightlots of weighton a vegetarian diet and many vegetarians are far too thin.

Giving up meat helps purge the body of toxins (pesticides, environmental pollutants, preservatives) that overload our systems and cause illness. When people begin formal detoxification programs, their first step is to replace meats and dairy products with fruits and vegetables and juices.

There are no studies showing that elimination of meat from the diet helps purge the body of toxins. The wording is interesting as it implies that vegetarianism will render a sinful body pure.

Most plant foods today are loaded with pesticides and many components in animal products support the bodys detoxification systemsuch as iron in meat, amino acids in bone broths, vitamin A in liver and saturated fat in butter.

No doubt about it, however, toxins are everywhere, in plant foods and animal foods. Health conscious consumers need to do their best to reduce the toxic load by choosing organic plant foods and pasture-raised animal foods.

The Honolulu Heart Study found an interesting correlation of Parkinsons disease with the consumption of fruit and fruit juices.16 Men who consumed one or more servings of fruit or fruit drinks per day were twice as likely to develop Parkinsons as those who consumed less fruit. Commentators proposed either high levels of pesticides or natural nerve toxins called isoquinolones that occur in fruit as the cause. Salicylates are another component of fruit that can lead to problems. So even the consumption of healthy fruit is not necessarily safe.

Its a wonderful thing to be able to finish a delicious meal, knowing that no beings have suffered to make it

Not a single bite of food reaches our mouths that has not involved the killing of animals. By some estimates, at least 300 animals per acreincluding mice, rats, moles, groundhogs and birdsare killed for the production of vegetable and grain foods, often in gruesome ways. Only one animal per acre is killed for the production of grass-fed beef and no animal is killed for the production of grass-fed milk until the end of the life of the dairy cow.

And what about the human beings, especially growing human beings, who are suffering from nutrient deficiencies and their concomitant health problems as a consequence of a vegetarian diet? Or does only animal suffering count?

Of course, we should all work for the elimination of confinement animal facilities, which do cause a great deal of suffering in our animals, not to mention desecration of the environment. This will be more readily accomplished by the millions of meat eaters opting for grass-fed animal foods than by the smaller numbers of vegetarians boycotting meat.

Vegetarians wishing to make a political statement should strive for consistency. Cows are slaughtered not only to put steak on the table, but to obtain components used in soaps, shampoos, cosmetics, plastics, pharmaceuticals, waxes (as in candles and crayons), modern building materials and hydraulic brake fluid for airplanes. The membrane that vibrates in your telephone contains beef gelatin. So to avoid hypocrisy, vegetarians need to also refrain from using anything made of plastic, talking on the telephone, flying in airplanes, letting their kids use crayons, and living or working in modern buildings.

The ancestors of modern vegetarians would not have survived without using animal products like fur to keep warm, leather to make footwear, belts, straps and shelter, and bones for tools. In fact, the entire interactive network of life on earth, from the jellyfish to the judge, is based on the sacrifice of animals and the use of animal foods. Theres no escape from dependence on slaughtered animals, not even for really good vegan folks who feel wonderful about themselves as they finish their vegan meal.

Vegetables are endlessly interesting to cook and a joy to eat. Its an ever-changing parade of flavors and colors and textures and tastes.

To make processed vegetarian foods taste delicious, manufacturers load them up with MSG and artificial flavors that imitate the taste of meat. If you are cooking from scratch, it is difficult to satisfy all the taste buds with dishes lacking animal foods. The umami taste is designed to be satisfied with animal foods.

In practice, very few people are satisfied with the flavors and tastes of a diet based exclusively on plant foods, even when these foods are loaded up with artificial flavors, which is why it is so difficult for most people to remain on a vegan diet. Vegetables are a lot more interesting and bring us a lot more joy when dressed with egg yolks and cream or cooked in butter or lard. But if you are a vegan, youll be using either liquid or partially hydrogenated vegetable oils, both extremely toxic.

Livestock farms create phenomenal amounts of waste, tons of manure, a substance thats rated by the Environmental Protection Agency (EPA) as a top pollutant. And thats not even counting the methane gas released by goats, pigs and poultry (which contributes to the greenhouse effect); the ammonia gases from urine; poison gases that emanate from manure lagoons; toxic chemicals from pesticides; and exhaust from farm equipment used to raise feed for animals.

The problem is not animals, which roamed the earth in huge numbers emitting methane, urine and manure long before humans came on the scene, but their concentration into confinement facilities. Only strong, committed, persistent and focused human effort will accomplish the goal of eliminating these abominationsthe kind of strength, commitment, persistence and focus that only animal foods rich in cholesterol, zinc, good fats and vitamin B12 can sustain. In nature and on old-fashioned farms, the urine and manure from animals is not a pollutant but a critical input that nourishes plant life. As for methane, the theory that methane from animals contributes to global warming is just thata theory, one that doesnt even pass the test of common sense.

Without urine and manure to nourish the soil, plant farmers need more pesticides, more chemicals. And theres only one way to eliminate exhaust from farm equipment used to raise plant foods for vegan dietspull those plows with horses and mules.

The average bone loss for a vegetarian woman at age 65 is 18 percent; for non-vegetarian women, its double that. Researchers attribute this to the consumption of excess protein. Excess protein interferes with the absorption and retention of calcium and actually prompts the body to excrete calcium, laying the ground for the brittle bone disease osteoporosis. Animal proteins, including milk, make the blood acidic, and to balance that condition, the body pulls calcium from bones. So rather than rely on milk for calcium, vegetarians turn to dark green leafy vegetables, such as broccoli and legumes, which, calorie for calorie, are superior sources

References, please?

The theory that excess protein causes bone loss was first presented in 196817 and followed up in 1972 with a study comparing bone density of vegetarians and meat eaters.18 Twenty-five British lacto-ovo vegetarians were matched for age and sex with an equal number of omnivores. Bone density, determined by reading X-rays of the third finger metacarpal, was found to be significantly higher in the vegetariansthese are lacto-ovo vegetarians, not vegans, so they will have good calcium intake.

Dr. Herta Spencer, of the Veterans Administration Hospital in Hines, Illinois, explains that the animal and human studies that correlated calcium loss with high protein diets used isolated, fractionated amino acids from milk or eggs.19 Her studies show that when protein is given as meat, subjects do not show any increase in calcium excreted, or any significant change in serum calcium, even over a long period.20 Other investigators found that a high-protein intake increased calcium absorption when dietary calcium was adequate or high, but not when calcium intake was a low 500 mg per day.21

So meat alone will not help build strong bones. But meat plus dairy is an excellent combination. The chart below illustrates the difficulty of obtaining adequate calcium from green leafy vegetables or legumes and contradicts the claim made above that leafy green vegetables and legumes supply more calcium on a per-calorie basis. The opposite is the case. The RDA for calcium can be met for under 700 calories using cheese or milk, but requires 1200 calories for spinach and 5100 calories for lentils. And not even the most dedicated vegetarians could choke down 13 cups of spinach or 32 cups of lentils (that would be almost doubled once the lentils were cooked) per day (see sidebar, below). Leafy greens present additional problems because they contain calcium-binding oxalic acid.

Calcium assimilation requires not only adequate protein but also fat-soluble vitamins A, D and K2, found only in animal fats. The lactoovo vegetarian consuming butter and full fat milk will take in the types of nutrients needed to maintain healthy bone mass, but not the vegan.

It takes 15 pounds of feed to get one pound of meat. But if the grain were given directly to people, thered be enough food to feed the entire planet. In addition, using land for animal agriculture is inefficient in terms of maximizing food production. According to the journal Soil and Water, one acre of land could produce 50,000 pounds of tomatoes, 40,000 pounds of potatoes, 30,000 pounds of carrots or just 250 pounds of beef.

No land anywhere in the world will produce 50,000 pounds of tomatoes, 40,000 pounds of potatoes or 30,000 pounds of carrots per acre year after year after year unless bolstered with fertilizer. Such land rotated with animal grazing will be fertilized naturally; without the manure and urine of animals, synthetics must be appliedsynthetics that require large amounts of energy to produce and leave problematic pollutants, such as fluoride compounds, as a by-product. And much of the worlds landmountainous, hillside, arid and marginal areasis incapable of producing harvestable crops even with a large fertilizer input. But this land will support animal life very well. Eliminating the animals on this land in order to produce vegetable crops will indeed create famine for the people who live there.

The EPA estimates that nearly 95 per cent of pesticide residue in our diet comes from meat, fish and dairy products. Fish, in particular, contain carcinogens (PCBs, DDT) and heavy metals (mercury, arsenic; lead, cadmium) that cannot be removed through cooking or freezing. Meat and dairy products are also laced with steroids and hormones.

Pesticides and heavy metals are found in animal foods only because they are applied to plant foods that feed the animals. Pasture-based livestock production and wild caught fish do not contribute to pesticide residue. Conventionally raised vegetables and grains are loaded with chemicals.

Vitamin A obtained in adequate amounts from animal foods provides powerful protection against dioxins like PCBs and DDT.23 Vitamin B12 is also protective. Good gut flora prevents their absorption. Humans have always had to deal with environmental carcinogenssmoke is loaded with themand heavy metals like mercury, which occur naturally in fish. We can deal with these challenges when we have adequate amounts of the nutrients supplied by animal foods.

According to the Center for Science in the Public Interest, which has stringent food standards, 25 per cent of all chicken sold in the United States carries salmonella bacteria and, the CDC estimates, 70 percent to 90 percent of chickens contain the bacteria campylobacter (some strains of which are antibiotic-resistant), approximately 5 percent of cows carry the lethal strain of E. coli O157:H7 (which causes virulent diseases and death), and 30 percent of pigs slaughtered each year for food are infected with toxoplasmosis (caused by parasites).

The most common source of food-borne illness by a long shot is fruits and vegetables.24 Problems with animal foods stem from factory farming practices. Milk, meat and eggs raised naturally do not present problems of food-borne illness.

Back pain appears to begin, not in the back, but in the arteries. The degeneration of discs, for instance, which leads to nerves being pinched, starts with the arteries leading to the back. Eating a plant-based diet keeps these arteries clear of cholesterol-causing blockages to help maintain a healthy back.

This item is pure speculation. One of the most common side effects of cholesterol-lowering is crippling back pain. The muscles that support our spine require animal foods to maintain their integrity. And the bones in our spine need a good source of calcium, namely dairy products or bone broth, to remain strong.

Eating a lot of vegetables necessarily means consuming fiber, which pushes waste out of the body. Meat contains no fiber. Studies done at Harvard and Brigham Womens Hospital found that people who ate a high-fiber diet had a 42 percent lower risk of diverticulitis. People who eat lower on the food chain also tend to have fewer incidences of constipation, hemorrhoids and spastic colon.

Konstantin Monastyrsky, author of Fiber Menace, begs to differ. He notes that because fiber indeed slows down the digestive process, it interferes with the digestion in the stomach and, later, clogs the intestines. The results of delayed indigestion (dyspepsia) include heartburn (GERD), gastritis (the inflammation of the stomachs mucosal membrane), peptic ulcers, enteritis (inflammation of the intestinal mucosal membrane), and further down the tube, constipation, irritable bowel syndrome, ulcerative colitis, and Crohns disease. Hemorrhoids and diverticulitis are other likely resultsscientific studies do not support the theory that fiber prevents these conditions.25

Plants, grains and legumes contain phytoestrogens that are believed to balance fluctuating hormones, so vegetarian women tend to go through menopause with fewer complaints of sleep problems, hot flashes, fatigue, mood swings, weight gain, depression and a diminished sex drive.

Lets see now, hormones in meat and milk are bad (see Item 13), but by tortured vegetarian logic, hormones in plant foods are good. Where is the research showing that vegetarian women go through menopause with fewer complaints? Numerous studies have shown that the phytoestrogens in soy foods have an inconsistent effect on hot flashes and other symptoms of menopause.26

The body needs cholesterol, vitamin A, vitamin D and other animal nutrients for hormone production. A vegetarian diet devoid of these nutrients is a recipe for menopausal problems, fatigue and diminished sex drivethe dietary proscriptions of the puritanical Graham and Kellogg work very well for their intended purpose, which is to wipe out libido in both men and women.

Lack of cholesterol, vitamin D and vitamin B12 is a recipe for mood swings and depression. If you want to have a happy menopause, dont be a vegetarian!

We spend large amounts annually to treat the heart disease, cancer, obesity, and food poisoning that are byproducts of a diet heavy on animal products.

We have commented on the link between vegetarianism and heart disease, cancer, obesity and food poisoning above. The main change in the American diet paralleling the huge increase in health problems is the substitution of vegetable oils for animal fats. A secondary change is the industrialization of agriculture. The solution to our health crisis is to return to pasture-based farming methods and the animal food-rich diets of our ancestors.

Because of our voracious appetite for fish, 39 per cent of the oceans fish species are over-harvested, and the Food & Agriculture Organization reports that 11 of 15 of the worlds major fishing grounds have become depleted.

Lets pass laws against overfishing! And lets provide the incentive to anti-overfishing activists by pointing out the important benefits of seafood in the diet.

It takes 2,500 gallons of water to produce one pound of mutton, but just 25 gallons of water to produce a pound of wheat. Not only is this wasteful, but it contributes to rampant water pollution.

Reference please?

If a sheep drinks one gallon of water per day which is a lotthe animal would only need about 600 gallons of water to yield almost eighty pounds of meat. Thats less than eight gallons of water per pound, much less than the water required to produce a pound of wheat.

If you set a good example and feed your children good food, chances are theyll live a longer and healthier life. Youre also providing a market for vegetarian products and making it more likely that theyll be available for the children.

You may not ever have any children if you follow a vegan diet, and in case you do, you will be condemning your kids to a life of poor health and misery. Heres what Dutch researcher P C Dagnelie has to say about the risks of a vegetarian diet: A vegan diet. . . leads to strongly increased risk of deficiencies of vitamin B12, vitamin B2 and several minerals, such as calcium, iron and zinc. . . even a lacto-vegetarian diet produces an increased risk of deficiencies of vitamin B12 and possibly certain minerals such as iron.27 These deficiencies can adversely affect not only physical growth but also neurological development. And following a vegan diet while pregnant is a recipe for disaster.

You will, however, by embracing vegetarianism, provide a market for vegetarian productsthe kind of highly processed, high-profit foods advertised in Vegetarian Times.

Vegetarian cooking has never been so simple. We live in a country that has been vegetarian by default. Our traditional dishes are loaded with the goodness of vegetarian food. Switching over is very simple indeed.

Going vegetarian is very difficult. The body needs animal foods and provides a powerful drive to eat them. Cravings and resentment are a natural byproduct of a vegetarian diet, not to mention separation from the the majority of humankind by unnatural eating habits and sense of moral rectitude.

Sidebars

by Russell Smith

Russell Smith, PhD, was a statistician and critic of the lipid heart theory of heart disease. He is the author of the massive Diet, Blood Cholesterol and Coronary Heart Disease: A Critical Review of the Literature (1991, Vector Enterprises), as well as The Cholesterol Conspiracy (Warren H. Green, Inc., 1991). As part of his efforts to reveal the flimsiness of the theoretical basis for the lipid hypothesis, he also looked at studies on vegetarianism in the scientific literature.

In a review of some 3,000 articles, Smith found only two that compared mortality data for vegetarians and nonvegetarians. One was a 1978 study of Seventh Day Adventists (SDAs) to which the above unreferenced claim probably refers. Two very poor analyses of the data were published in 1984, one by H. A. Kahn and one by D. A. Snowden.3 The publication by Kahn rather arbitrarily threw out most of the data and considered only subjects who indicated very infrequent or very frequent consumption of the various foods. The author then computed odds ratios which showed that mortality increased as meat or poultry consumption increased (but not for cheese, eggs, milk or fat attached to meat). When Smith analyzed total mortality rates from the study as a function of the frequencies of consuming cheese, meat, milk, eggs and fat attached to meat, he found that the total death rate decreased as the frequencies of consuming cheese, eggs, meat and milk increased. He called the Kahn publication yet another example of negative results which are massaged and misinterpreted to support the politically correct assertions that vegetarians live longer lives.

The Snowden analysis looked at mortality data for coronary heart disease (CHD), rather than total mortality data, for the 21-year SDA study. Since he did not eliminate the intermediate frequencies of consumption data on meat, but did so with eggs, cheese and milk, this analysis represents further evidence that both Kahn and Snowden based their results on arbitrary, after-the-fact analysis and not on pre-planned analyses contingent on the design of their questionnaire. Snowden computed relative risk ratios and concluded that CHD mortality increased as meat consumption increased. However, the rates of increase were trivial at 0.04 percent and 0.01 percent respectively for males and females. Snowden, like Kahn, also found no relationship between frequency of consumption of eggs, cheese and milk and CHD mortality risk.

Citing the SDA study, other writers have claimed that nonvegetarians have higher all-cause mortality rates than vegetarians4 and that, There seems little doubt that SDA men at least experience less total heart disease than do others. . .5 The overpowering motivation to show that a diet low in animal products protects against CHD (and other diseases) is no better exemplified than in the SDA study and its subsequent analysis. While Kahn and Snowden both used the term substantial to describe the effects of meat consumption on mortalities, it is obvious that trivial is the appropriate descriptor. It is also interesting to note that throughout their analyses, they brushed aside their totally negative findings on foods which have much greater quantities of fat, saturated fat and cholesterol.

The second study was published by Burr and Sweetnam in 1982.6 It was shown that annual CHD death rate among vegetarians was only 0.01 percent lower than that of nonvegetarians, yet the authors indicated that the difference was substantial.

The table below presents the annual death rates for vegetarians and nonvegetarians which Smith derived from the raw data in the seven-year Burr and Sweetnam study. As can be seen, the marked difference between vegetarian and nonvegetarian men in Ischemic Heart Disease (IHD) was only .11 percent. The difference in all-cause death rate was in the opposite direction, a fact that Burr and Sweetnam failed to mention. Moreover, the IHD and all-cause death rates among females were actually slightly greater for heart disease and substantially greater for all causes in vegetarians than in nonvegetarians.

These results are absolutely not supportive of the proposition that vegetarianism protects against either heart disease or all-cause mortalities. They also indicate that vegetarianism is more dangerous for women than for men.

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by Jim Earles

VEGETARIANISM: In its simplest form, the abstinence from all flesh foodsthose foods which inherently require the taking of an animals lifein favor of plant foods. Without further qualifying terms, the term vegetarian does not specify whether or not a person might choose to eat animal products like milk and eggs, which do not inherently require the taking of an animals life.

LACTO-VEGETARIANISM: A vegetarian diet with the inclusion of milk and/or dairy products.

OVO-VEGETARIANISM: A vegetarian diet with the inclusion of eggs (usually eggs from chickens or other fowl, but presumably an ovo-vegetarian might also eat fish roe).

PESCO-VEGETARIANISM (a.k.a. pescetarianism): A vegetarian diet with the exception of consuming fish and/or seafood. This is often viewed by adherents as being a voluntary abstention from eating land animals. This diet is similar to (and often overlaps with) the popular version of the Mediterranean Diet.

POLLO-VEGETARIANISM (a.k.a. pollotarianism): A vegetarian diet with the exception of consuming chicken (and possibly other types of fowl). This is often viewed by adherents as being a voluntary abstention from red meats and from eating more highly-developed mammals such as cows, pigs, sheep, etc. NOTE: Many vegetarians do not feel that people who include seafoods or land fowl in their diets qualify as vegetarians at all. Indeed, many practicing pescetarians and pollotarians feel that their diet is a similar but entirely distinct dietary philosophy from vegetarianism. Some people prefer to use terms such as semi-vegetarianism or flexitarianism to refer to the primary (but not exclusive) practice of vegetarianism. ALSO NOTE: The above variants on vegetarianism may be combined in any way to describe an individuals food choices. (e.g. lacto-ovo-vegetarianism, pollo-ovo-vegetarianism, etc.)

VEGANISM: The more extreme end of the scale of vegetarianism. A vegan (both vee-gan and vay-gan are accepted pronunciations) abstains from all animal foods, including any meats, fish, eggs or dairy. Some vegans, but not all of them, also abstain from honey and other bee products, as well as clothing and materials made from animal products (e.g. silk, leather, fur, etc.). Many vegans view their dietary choices as being just a part of veganism, which is more fully viewed as a way of life and a socio-political stance.

FREEGANISM: A subset of veganism which utilizes the same basic food choices but often lives out the socio-political aspects of veganism in an even more direct and radical way. Freegans seek to minimize or eliminate participation in the corporate food system by practices such as foraging for wild plant foods, community gardening, bartering for food instead of using money and dumpster diving (taking food that is still edible but past its expiration date out of supermarket, restaurant and bakery dumpsters). Dumpster diving especially is seen as a radical form of environmental stewardshipsaving otherwise good food from going to a landfill. Getting food for free in this way also gives rise to the namefree plus vegan equals freegan.

MEAGANISM: A further subset of freeganism! A meagan would dispense with the strict adherence to a vegan diet when their dumpster diving provides them with usable meat or other animal foods. (Meat plus vegan equals meagan.) Some meagans argue that all foods produced by the dominant corporate model are ethically-tainted, meatless or otherwise. Following this line, there is no moral high ground to be had when eating salvaged food. Other meagans believe that it is disrespectful to the spirit of an animal to allow its flesh or other products to be wasted, so it is better to eat these items and honor the loss of their lives by keeping them in the food chain whenever possible.

FRUITARIANISM: A subset of veganism wherein neither animals nor plants are allowed to be harmed or killed to feed human beings. This means that only the fruits of plants and trees are morally acceptable as human food, as these may be harvested without doing any harm to the plant. However, there is no strong consensus among fruitarians as to what exactly should constitute fruit. Botanically speaking, some common vegetables are actually classified as fruits (such as bell peppers, tomatoes and cucumbers), as are nuts and grains. Some fruitarians abide by the wider, botanical meaning of fruit, while others only eat the sweet, fleshy, more commonly-known fruits. Many fruitarians also include seeds in their diet, following the line of thought that anything that naturally falls from a plant (or would do so) is valid food.

LIQUIDARIANISM / JUICEARIANISM: A rarely-espoused dietary philosophy wherein adherents only consume liquids and fruit and vegetable juices. More often than not, such a program would only be undertaken for a limited period of time only for the purposes of a cleansing fast. However, a relatively small number of people have attempted to maintain such a regime over an indefinite period of time.

RAW FOODISM: While not necessarily falling under any of the above headings, many raw foodists base their food choices on some form of vegetarianism or veganism. A raw foodist consumes most or all of their foods in uncooked and unprocessed forms. (This may or may not include practices such as the soaking of nuts, seeds and grains.) While many raw foodists minimize or exclude animal products, some do consume raw meats, eggs and dairy products.

MACROBIOTICS: Again not necessarily falling under any vegetarian category, but many macrobiotic adherents have strong overlap with vegetarianism and veganism. The macrobiotic diet emphasizes eating foods that are grown locally and (to the extent possible) when they are actually in season, placing an emphasis on eating grains, legumes, vegetables, fruits, nuts, seeds, fermented soy products and sometimes fish. Processed foods and animal products are typically excluded, as are vegetables of the nightshade family.

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Twenty-Two Reasons Not to Go Vegetarian

Vegetarianism: Pros and Cons – GOQii

The philosophy around going meatless or adopting a vegetarian lifestyle has become increasingly popular. People are being more aware of foods that are nutrient dense (and those less so) which helps them to stay healthy and fit. So is veering towards a plant-based approach the best way to go? A growing number of people seem to think so. A Vegetarian resource group conducted a poll and found that there was rise in people adopting vegetarianism/veganism compared to previous years data in USA, similar data was shown for Europe, Israel and India as well.

Before we fall in to the discussion of Should people become Vegetarian? however, its important to understand what vegetarianism actually means as well as the benefits and potential risks associated with it.

Vegetarian broadly refers to those who restricts consumption of animal products like meat, fish, poultry etc., and largely rely on plant based foods like fruits, veggies, whole grains, dairy, pulses etc., for living. Within this group, there are various levels of vegetarians. These are classified from most restrictive to those who are less so.

A vegetarian diet is naturally low in fats and high in fiber, but being vegetarian has its own risks. So no matter at what level you happen to fall, and no matter what reason you have chosen to commit to it , there are both pros and cons of being vegetarian. Here are few of them:

Pros of Vegetarianism:

Cons of Vegetarianism:

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Vegetarianism: Pros and Cons - GOQii

Proven Advantages And Disadvantages Of Vegetarianism

The vegetarian diet is not a new concept but it has been made into one. Since the time immemorial, the cry that the human beings must return to the vegan lifestyle has been echoing in all the places around the world. But some hypocrites have remodeled the claims into something that is very new. It has been said that the vegetarian diet is the most preferred diet all over the world. The vegetarian form of the diet is the most preferred and the most trusted form of the diet in the world. But the parents have expressed duel of the nutritional intake in the vegetarian foods. But the dietary experts have consoled the parents that the well planned and the careful selection of the foods will provide the same amount of the nutrients that the meat based foods provide. But extra care must be provided to the children if the children do not consume enough of meat and dairy products. The nutritional needs of the children differs as they advance in years.

There are the number of reasons for a person to become a vegetarian. Some people adapt the vegetarian lifestyle for health reasons while others adopt it because they have been born or brought up in a vegan family. Even cultural issues also plays a role in making a man to adopt the vegetarian lifestyle. The concern and love for the animals also has a lot to do for the community or a family to become vegans.

Most people are of the opinion that the vegetarian diets are devoid of the proteins and the fats that the animal meat possess. But it is not true. The vegetarian diet also possess these kinds of the nutrients and the people need to carefully select the foods that are rich in them. The meat contains unsaturated fats and cholesterol and these harm the body.

The vegetarianism has been said to be the act of abstaining from all kinds of meat that is obtained from animal slaughter and living exquisitely only on the foods prepared by the dairy products, vegetables, nuts, seeds, pulses, fruits and grains. Some vegetarians include the eggs as a part of their daily diet while others do not. Various pros and cons of Vegetarianism are listed here.,

There are many benefits as opposed to the disadvantages of being a vegetarian. But the scientists have forestalled the people by telling them that they have also found that the intake of the vegetarian foods also increases the risks of developing calories. But not that alone, an estimated amount of the diseases like the cancers and other chronic diseases all owe their allegiance to the bad diets. So this has to be addressed and proper eating habits must be enforced. The advantages of vegetarianism are,

Though the advantages of being a vegan is very obvious, there are also some or the other complications that needs to be addressed in order to obtain a clear picture of the mode of the foods that may be eaten. Some people shriek from the idea of the meat free diet. So there are some demerits/cons of vegetarianism also listed here.

The term vegetarianism is a broad one and it does not confine one to a single aspect. The vegetarian people and the others need to understand the various categories that exists between the vegans. The types of the vegetarian foods depend on the selection of the foods and the types get classified according to it. As of now, it has said that there are four types of the vegetarian people. They are as follows :

The people who follow this type of the vegetarianism will live only on the food items like the dairy products, eggs and the usual plants for food. This is the most common form of the vegetarianism. They do not consume any animal products nor use them.

The people who follow this type of the vegan style will only include eggs and the plant based foods into their daily food regime. These people too do not consume meat products. They do not eat dairy products too.

These people eat the plant based foods as the above said groups of the people and they also consume the dairy products. These people are said to be the perfect types of the vegetarians.

These kind of the people eat only plant based foods and they neither include meat and dairy foods.

There is another category of the people who do not consume the red meat but eat the fish along with the plant based foods.

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Proven Advantages And Disadvantages Of Vegetarianism

Anti-Aging Medical Training – AAOPM

Throughout the aging process, our internal systems and body chemistry change, and we develop certain imbalances and deficiencies, which in the past we would explain away as caused by life changes and genetics. Today we are able to review these various primary and secondary hormones, through testing and systems reviews, and to develop an effective personalized treatment plan that reverses these chronic conditions.

Anti-Aging medicine is an extension of preventive health care. If you are testing your patients cholesterol, or prescribing lipid-lowering drugs, melatonin or DHEA, or suggesting a mammogram, you are already involved in certain aspects of Anti-Aging medicine. It is estimated that more than 90% of all adult illness is due to the generative processes of aging, which may be corrected or improved by the addition of supplements, detoxification and hormonal correction.

Anti-Aging is a relatively new field of medicine, where natural approaches and lifestyle changes are used, in conjunction with traditional medicine, where applicable, to give relief to a variety of conditions.

During the Anti-Aging training course, you will understand how to analyze, test, evaluate and treat numerous chronic conditions you are presented from patients with each day. Attendees will be evaluated based upon specific criteria, and, upon the successful completion of the Anti-Aging & Regenerative Medical Training Workshop, will be awarded A.A.O.P.Ms certification certificate.

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Anti-Aging Medical Training - AAOPM