Newswise Sivaguru (Siva) Jayaraman, Ph.D., associate professor of chemistry and biochemistry at North Dakota State University, Fargo, has received a three-year, $429,500 award from the National Science Foundation (NSF) to conduct research outlined in his proposal titled Light Induced Enantiospecific Chiral Transfer in Solution. The funding also provides research opportunities to graduate and undergraduate students to develop environmentally benign, green strategies to perform chemical reactions.

The research program in Dr. Sivas group focuses on using light to transfer molecular chirality in photochemical reactions (reactions initiated by light) to produce molecules that are chiral (have two non-superimposable mirror images) and make only one of the two possible forms (a single enantiomer).

Based on the funding from the National Science Foundation, his research group will study light-induced enantiospecific chiral transfer in solution. One of the research goals is to gain a fundamental understanding of interaction of light with photoreactive substrates, coupled with an intricate control over molecular reactivity, dynamics and non-bonding interactions to enhance stereoselectivity in the photoproducts.

Synthesizing chiral compounds with high stereoselectivity during light-induced transformations provides an opportunity to develop sustainable strategies with minimal impact on the environment, said Dr. Jayaraman.

Students learn how modern chemical methods can be used for synthesizing compounds with minimal environmental impact. With this most recent NSF funding, students involved in the proposed investigations will learn both traditional techniques to characterize and evaluate asymmetric induction during enantiospecific phototransformations and modern spectroscopic methods and characterization techniques to assess excited state reactivity.

The award is a renewal grant of Dr. Jayaramans CAREER award, which includes research opportunities for NDSU students. His research also provides opportunities to area high school students through a program called PICNICS (Parents Involvement with Children, Nurturing Intellectual Curiosity in Science).

As part of the PICNICS program, top area high school students conduct a variety of research each summer alongside graduate students and postdoctoral fellows at the Department of Chemistry and Biochemistry, NDSU, Fargo. The PICNICS program was developed by Dr. Jayaraman as an outreach component in his NSF CAREER award to engage high school students and their parents about recent science and technology advancements and to encourage high school juniors and seniors to consider science as a career path.

Dr. Sivaguru (Siva) Jayaraman joined the faculty at NDSU in 2006. He was promoted to associate professor in 2011. He previously received an NSF CAREER award in 2008, a Grammaticakis-Neumann Prize from the Swiss Chemical Society in 2010, a Young-investigator award from the Inter-American Photochemical Society (I-APS) in 2011, and a Young-investigator award from Sigma Xi in 2012.

At NDSU, Dr. Jayaraman received the 2010 Excellence in Research Award, 2011 Excellence in Teaching award and 2012 Peltier Award for Innovation in Teaching. He completed a post-doctoral fellowship at Columbia University, New York, N.Y., after receiving his Ph.D. from Tulane University, New Orleans, La. He received a masters degree in chemistry from the Indian Institute of Technology, Madras, India, and completed a bachelors degree in chemistry from St. Josephs College, Bharathidasan University, Trichy, India.

For more info regarding Dr. Sivaguru Jayaramans research, teaching and outreach visit http://sivagroup.chem.ndsu.nodak.edu/

Excerpt from:
NDSU Faculty Receives NSF Funding for Chemistry Research

Anton Iliuk never expected to be an entrepreneur.

Now, the former Purdue University biochemistry students doctoral project to develop new technology that can help pinpoint potential targets for cancer therapy has transformed into a growing startup in Purdue Research Park.

Iliuks former adviser, biochemistry associate professor W. Andy Tao, is his business partner.

Most science majors have two paths, Iliuk said. One is academia. One is industry. This is the path less traveled. Im not a business guy.

But the companys first product, PolyMAC, still managed to generate sales of nearly $50,000 in five months for his company, Tymora Analytical Operations LLC.

Id like to turn this into a multimillion-dollar company, Iliuk said. If you dont believe, nobody else will.

Iliuk, the companys president and chief technology officer, said a realistic goal for next year would be to double the sales of PolyMAC, which analyzes tissue modification on a cellular level.

You send in a fishing net, you try to pick up everything there is, sort through it and see what has changed from normal tissue to cancer tissue, Iliuk said.

The next step for Tymora is to get its next product, pIMAGO, to market. Iliuk said the goal of pIMAGO is to cut the cost associated with the early stages of drug development by showing which drugs will be more effective.

Its sort of a launch pad, Iliuk said. Were trying to improve the way people do lab research.

Originally posted here:
Purdue grad hopes to grow Tymora startup into 'multimillion-dollar company'

Public release date: 22-Aug-2012 [ | E-mail | Share ]

Contact: Garth Hogan ghogan@asmusa.org American Society for Microbiology

Andrew Lee Lovering, Ph.D., School of Biosciences, University of Birmingham, has received a 2012 ICAAC Young Investigator Award for his seminal work on the structural biology and biochemistry of the proteins that synthesize and modify cell walls in bacteria. Natalie Strynadka, University of British Columbia, describes the significance of Lovering's work: "his spectacular abilities in structural biology clearly paved the way for our understanding of these important antibacterial targets which are also membrane-anchored, a hurdle that has thwarted literally decades of attempts at previous characterization by many groups worldwide." "His protein structure work has shown how Gram positive bacteria synthesize teichoic acids, how bacterial cell walls are transglycosylated, and how enzymes of predatory bacteria partially degrade bacterial cell walls as they invade prey bacteria," explained nominator Liz Sockett, University of Nottingham.

Lovering obtained his B.Sc. in Biochemistry from Birmingham University, where he also earned his Ph.D. in Biosciences. There he used x-ray crystallography to detail the mechanism of action of two enzymes involved in cancer therapies; one a bacterial nitroreductase used in gene therapy of solid tumors, and the other a target for a cell differentiation approach tackling acute myeloid leukemia.

After graduating from Birmingham University, a postdoctoral position in Strynadka's laboratory at the University of British Columbia introduced Lovering to the subject of antibacterial research. This led to determination of the structures of two monotopic membrane proteins involved in bacterial cell wall synthesis. One of these, S. aureus PBP2, represented the first detailed view of how bacteria catalyze the essential step of peptidoglycan polymerisation, a potentially excellent drug target. The other, S. epidermidis TagF, revealed how the Gram-positive wall polymer teichoic acid is synthesized and may form the basis for the development of antivirulents. The PBP2 publication was chosen as one of the highlights of the year by Science and C&E News.

Since establishing his own research group in 2010, Lovering's focus has shifted to deciphering the molecular basis of bacterial predation by Bdellovibrio bacteriovorus, a phenomenon that may lead to its exploitation as a "living antibiotic". In collaboration with Sockett at the University of Nottingham, this approach has already begun to detail how the invading bacterium modifies the prey cell wall for purposes of niche formation, and also how Bdellovibrio and other bacteria hydrolyze the ubiquitous bacterial second messenger cyclic-di-GMP. "As invited speaker of the 2012 Gordon Conference on Bacterial Sensory Transduction, he described the first ever crystal structure of an HD-GYP bacterial signaling protein," says Sockett.

"Lovering's enthusiasm and fascination with the microbial world is always palpable. His level of insight, profound knowledge of fundamental biochemistry, and ability to see connections that others would have missed never fail to amaze me," summarizes Klaus Ftterer, University of Birmingham. "As he builds his research group it is clear that his work will enlighten our understanding of an unusual microorganism, and his enthusiasm will inspire junior researchers in both the structural biology and microbiology communities."

Strynadka agrees, "he is highly collegial, modest, and a natural teacher. His love of and interest in science is truly infectiousknowledge he loves to share with others. Collectively, I believe him to be a truly exceptional rising star who will continue to make fundamental advances to structural microbiology."

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The ICAAC Young Investigator Award will be presented during ASM's 52nd Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC), September 9-12, 2012 in San Francisco, CA. ASM is the world's oldest and largest life science organization and has more than 40,000 members worldwide. ASM's mission is to advance the microbiological sciences and promote the use of scientific knowledge for improved health, economic, and environmental well-being.

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The American Society for Microbiology honors Andrew Lovering

Public release date: 13-Aug-2012 [ | E-mail | Share ]

Contact: Angela Hopp ahopp@asbmb.org 240-283-6614 American Society for Biochemistry and Molecular Biology

A research team at the University of California, Davis, has found that important and resourceful bacteria in the baby microbiome can ferret out nourishment from a previously unknown source, possibly helping at-risk infants break down components of breast milk.

Breast milk is amazingly intricate, providing all of the nutrients necessary to sustain and strengthen infants in the first months of life. Moreover, this natural source of nutrition provides protection from infections, allergies and many other illnesses.

Breast milk also promotes the growth of protective bacteria in an infant's intestine. Because breast milk contains glycans (complex sugars) that infants cannot breakdown, it promotes the growth a specific type of bacteria, called bifidobacteria, that can process these glycans. While it is known that bifidobacteria avail themselves of the free glycans in breast milk, it was not known whether these bacteria could also obtain glycans that were linked to proteins. Such proteins are called glycoproteins, and they are abundant in breast milk.

The research team led by David A. Mills at the UC-Davis investigated the ability of bifidobacteria to remove glycans from milk glycoproteins. Their work was recently published in the journal Molecular & Cellular Proteomics.

Mills' group found that specific strains of bifidobacteria possessed enzymes capable of removing glycan groups from glycoproteins, enabling them to use these glycans as an additional food source. Surprisingly, one of the enzymes, EndoBI-1, was able to remove any type of N-linked glycan (glycans attached to proteins by the amino acid asparagine). This is unique among enzymes of this type and may provide a growth advantage for bifidobacteria in the infant intestine because the glycoproteins in breast milk have complex glycans attached.

Mills explains that the ability of EndBI-1 to remove a variety of complex N-linked glycans combined with its unusual heat stability make "this potentially a very useful tool in both food processing and proteomics/pharmaceutical research."

The team's work suggests that bifidobacteria do not primarily feed on the glycans from milk glycoproteins. However, the study did show that under the proper conditions bidfidobacteria can grow when protein-linked glycans are the only energy source.

"One obvious goal of this research is to find ways to translate the benefits provided by milk and bifidobacteria to at risk populations such as premature infants, malnourished children, among many others," Mills says.

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Protective bacteria in the infant gut have resourceful way of helping babies break down breast milk

ASHBURN, Va. (AP) -- Lorenzo Alexander has quite a collection of white bottles, labeled with words straight from a biochemistry class. Beta Alanine Supreme. Carnitine Synergy. Uber C. Some 19 containers, big and small, in his Washington Redskins locker.

''I have a lot of supplements,'' he said.

The consummate self-made NFL player, Alexander has always been conscious about his diet. Like many players, he also gets advice on the right mix of tablets to maximize his endurance and energy output. Or, as he puts it, ''to help balance your body out.''

This year, it's been more of a challenge to find that balance. Alexander, who once was a 300-pound lineman, arrived at training camp weighing 245, having dropped some 30 pounds from this time last season so that he can hold his own in his new role as the team's primary backup at inside linebacker.

''Being 265,'' he said, ''is not ideal for covering tight ends and fast wide receivers down the middle of the field.''

No one would expect anything different from the player who arrived as a practice squad nobody in 2006 and soon became an indispensable utility man, working his way up to his current role as a team captain who now gets annual support from his teammates as an ought-to-be Pro Bowl player.

''I'd say he's one of, if not the biggest influence I've had since I've been here,'' said linebacker Ryan Kerrigan, a first-round draft pick last year. ''He seems to me what really embodies a professional. Not just a professional athlete, but a professional human being. He shows you what hard work can do.''

Alexander was a novelty his rookie season, a three-way player who saw game action on the offensive line, defensive line and special teams. He made his name with hard work, smarts and big special teams hits.

In 2010, the Redskins (No. 25 in the AP Pro32) moved him to outside linebacker. Last year, he started learning the inside linebacker position. This year, it's his main focus on the only experienced alternative to starters London Fletcher and Perry Riley in the 3-4 scheme.

Alexander's weight loss has been noticeable during training camp. He broke up a pass over the middle to Santana Moss during Wednesday's practice, the type of play he couldn't have made when he was a lot heavier.

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Redskins' Alexander shrinks to play linebacker

NASA-JPl / Reuters

This artist's concept depicts the moment that NASA's Curiosity rover touches down onto the Martian surface

Barreling in from space at 13,000 mph before stopping a mere 25 feet above the ground would make anyone want to catch their breath, and NASAs Curiosity rover is no exception. Now that the Seven Minutes of Terror is over, the compact-car-sized biochemistry lab is spending its first two weeks doing the same thing you might do after stepping off a hair-raising roller coaster: making sure its parts are where theyre supposed to be and functioning correctly.

That means daily surprises, as technicians at the Jet Propulsion Laboratory in La Canada Flintridge, Calif., raise antennas, activate cameras, and gradually bring systems on line. Among the early treats: 297 black-and-white thumbnail pictures, which NASA processed into a low-quality video showing the final two-and-a-half minutes of Curiositys stomach-churning plunge through the Martian atmosphere. The thumbnails, though grainy, show the protective heat shield dropping away, the bumps from the rovers parachute descent, and dust kicking up as cables lowered the rover to the Martian surface. Scientists expect to have a full-resolution video from Curiositys descent imager in a few days.

(PHOTOS: An Inside Look at the Mars Curiosity Rover)

The rover also sent a new postcard: the first full-color landscape image of Curiositys Gale Crater home, taken as part of a focus test to check one of the cameras mounted on the rovers mast. Until this week the camera, called the Mars Hand Lens Imager (MAHLI),hadnt moved its focal components since July 2011four months before Curiosity launched. Even now, with the mast still tucked horizontally atop the rovers front left shoulder, the cameras initial focus test offers a tempting glimpse of the north wall of the rim at Gale Crater.

But thats just a small taste of what this particular camera, one of 17 aboard Curiosity, will provide once the mast is lifted and extended, especially once the cameras clear dust covers lift away. Its so awesome because we can put this camera anywhere, says Ken Edgett of Malin Space Science Systems in San Diego, which operates the camera. Up, down, within an inch of the soil, underneath the rover, anywhere. Itll extend up above the mast to give us the giraffes-eye view, or give us the oblique, dogs-eye view across the Martian surface. This camera can look wherever we want.

Many of this weeks most captivating images havent come from Curiosity but a high-resolution camera aboard the Mars Reconnaissance Orbiter, another player on NASAs robotic exploration team. One day after capturing a stunning shot of Curiosity parachuting towards Martian surface, the Orbiter executed an unusual 41-degree roll to deliver a fascinating crime scene image taken by a high-resolution camera aboard the Mars Reconnaissance Orbiter some 186 miles above the surface. The view offers a look at the pimple-sized rover in relation to the locations where Curiositys heat shield, parachute, back shell, and ballyhooed sky crane crash-landed after dropping away from the rover during its descent.

(Cover Story: Live From Mars)

Simply put, theyre all in the same Gale Crater neighborhood. The heat shield is farthest from Curiosity, about three-quarters of a mile away. Both the back shell and sky crane wound up about four-tenths of a mile from the rover. Of particular visual interest is a jagged pattern in the Martian soil to one side of the downed sky crane. Those dark areas downrange are the disturbed dust, says Sarah Milkovich, a JPL scientist. Its the same pattern we see when we have meteorites forming impact craters on the surface of a planetary body. Since the impacts from the spacecrafts components kicked up plenty of dust as well, Milkovich says future images should have even greater resolution. The Orbiter will again aim its cameras at Gale Crater in a few days, possibly for color photos.

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After the Descent: Mars Rover Preps for Thrilling Expedition

The American Society of Biochemistry and Molecular Biology (ASBMB) named Caltech chemistry professor Shu-ou Shan a recipient of the 2013 Young Investigator Award. The award will be presented at the ASBMB annual meeting in Boston next April.

Shan was recognized for her research that addresses how "a novel class of nucleotide hydrolases drives the efficient and accurate delivery of newly synthesized proteins to their correct destinations."

"This award would not have been possible without the support from my subgroup and division and all the wonderful Caltech students and postdocs who work so hard," says Shan.

"We are extremely happy that ASBMB has selected Shu-ou Shan for the Young Investigators Award," said Jacqueline Barton, Arthur and Marian Hanisch Memorial Professor, professor of chemistry, and chair of the Division of Chemistry and Chemical Engineering at Caltech. "It is a testament to the hard work and dedication of Shan and her team here at Caltech."

Shan's research interfaces between chemistry and biology to understand fundamental cellular processes at the level of chemical and physical principles. More information about Shan's research group at Caltech can be found at http://shangroup.caltech.edu.

The ASBMB Young Investigator Award recognizes outstanding research contributions to biochemistry and molecular biology. The recipient must have no more than 15 years postdoctoral experience. Nominations for these awards are made by ASBMB members, but nominees need not be members. The award consists of a plaque, $5,000, transportation, and expenses to present a lecture at the 2013 ASBMB annual meeting.

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Caltech Chemist Wins ASBMB Young Investigator Award

Aug. 1, 2012

Susan Henry wins prestigious award in lipid biochemistry

Susan Henry, professor of molecular biology and genetics and the Ronald P. Lynch Dean of the College of Agriculture and Life Sciences (CALS) from 2000 to 2010, won the 2013 Avanti Award in Lipids, according to the August issue of the magazine of the American Society for Biochemistry and Molecular Biology, ASBMB Today.

The award recognizes outstanding research contributions in the area of lipids, naturally occurring molecules that are structural components of cell membranes involved in energy storage and signaling. Henry is noted for her research on regulation of lipid metabolism and lipid-mediated signaling, using yeast as a model system.

A fellow of the American Association for the Advancement of Science and the American Academy of Microbiology, Henry is also past chair of the National Institutes of Health Advisory Committee on Research on Minority Health.

As part of the honor, Henry has been invited to present a lecture at the 2013 ASBMB Annual Meeting, which will be held in Boston in April 2013.

##

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Susan Henry wins prestigious award in lipid biochemistry

Edward A. Dennis is Distinguished Professor of Chemistry and Biochemistry, and of Pharmacology in the School of Medicine at UCSD. He received his BA from Yale University in 1963 and a Ph.D. from Harvard University in 1967, a Doctorate in Medicine (honorary) from Goethe University in Frankfurt in 2008, and he served as a Research Fellow at Harvard Medical School 1967-69.

Edward Dennis

At UCSD, Dr. Dennis has served as Chair of the Department of Chemistry and Biochemistry, Chair of the Faculty Academic Senate, and on the Board of Overseers. He has also been Visiting Professor at several universities and is an adjunct professor at The Scripps Research Institute. He has authored 350 research publications, patented 15 inventions, and edited 13 books. Dr. Dennis was named an inaugural Fellow of the American Association for the Advancement of Science (AAAS) in 1984, and was the recipient of the American Society of Biochemistry and Molecular Biologys Avanti Award in Lipid Enzymology in 2000, the European Federation for Lipid Science and Technologys European Lipid Science Award in 2007, and Yale Universitys Yale Medal in 2008.

What brought you to La Jolla? On Jan. 1, 1970 I started on a cross-country drive to a little village on the other ocean for my first job as an assistant professor in the formative days of UCSD. It was a great move and I never looked back.

What are your favorite places to go in La Jolla? I enjoy walking on the La Jolla Shores beach, the Coast Walk cliff and alongside La Jolla Cove.

If you could snap your fingers and have it done, what might you add to improve La Jolla? Rebalance the human and animal interests in the Cove.

Who or what inspires you? Im inspired by the creativity, curiosity, and inventiveness of the many outstanding educational/research institutions of La Jolla.

If you hosted a dinner party for eight, whom (living or deceased) would you invite? It would be a potluck six-course dinner, hosted by my wife and I with six memorable chefs, both past and present, each bringing their favorite dish. The list of chefs includes Julia Child, Pierre Troisgros, Tetsuya Wakuda, Alex Atala, Eric Pras and Thomas Keller.I

Tell us about what you are reading. The Entrepreneurial President, a recently published book about the leadership of Dick Atkinson, former Chancellor of UCSD and president of the University of California.

What would be your dream vacation? A flying tour of the greatest vineyards of the world starting in California and progressing south to Argentina and Chile, west to New Zealand, across Australia, on to South Africa, then to Germany, and finally, France.

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Edward Dennis of La Jolla takes scholarly approach to his long career in science

In an advance that could be used in masks to protect against nerve gas, scientists are reporting development of proteins that are up to 15,000 times more effective than their natural counterpart in destroying chemical warfare agents. Their report appears in ACS' journal Biochemistry.

Frank Raushel, David Barondeau and colleagues explain that a soil bacterium makes a protein called phosphotriesterase (PTE), which is an enzyme that detoxifies some pesticides and chemical warfare agents like sarin and tabun. PTE thus has potential uses in protecting soldiers and others. Natural PTE, however, works against only one of the two molecular forms of these chemical warfare agents, and it happens to be the less toxic form. The scientists thus set out to develop new versions of PTE that were more effective against the most toxic form.

To improve the enzyme's activity, Raushel and colleagues used an approach called "directed evolution." This technique imitates the way natural selection leads to improved forms of the biochemical substances in living things. In using directed evolution, the team made small random changes to the natural enzyme's chemical architecture and then tested resulting mutant enzymes for their ability to break down nerve agents. They isolated several mutants that fit the bill, including one that proved to be 15,000 times more effective than the natural enzyme.

More information: Enzymes for the Homeland Defense: Optimizing Phosphotriesterase for the Hydrolysis of Organophosphate Nerve Agents Biochemistry, Article ASAP. DOI: 10.1021/bi300811t

Abstract Phosphotriesterase (PTE) from soil bacteria is known for its ability to catalyze the detoxification of organophosphate pesticides and chemical warfare agents. Most of the organophosphate chemical warfare agents are a mixture of two stereoisomers at the phosphorus center, and the SP-enantiomers are significantly more toxic than the RP-enantiomers. In previous investigations, PTE variants were created through the manipulation of the substrate binding pockets and these mutants were shown to have greater catalytic activities for the detoxification of the more toxic SP-enantiomers of nerve agent analogues for GB, GD, GF, VX, and VR than the less toxic RP-enantiomers. In this investigation, alternate strategies were employed to discover additional PTE variants with significant improvements in catalytic activities relative to that of the wild-type enzyme. Screening and selection techniques were utilized to isolate PTE variants from randomized libraries and site specific modifications. The catalytic activities of these newly identified PTE variants toward the SP-enantiomers of chromophoric analogues of GB, GD, GF, VX, and VR have been improved up to 15000-fold relative to that of the wild-type enzyme. The X-ray crystal structures of the best PTE variants were determined. Characterization of these mutants with the authentic G-type nerve agents has confirmed the expected improvements in catalytic activity against the most toxic enantiomers of GB, GD, and GF. The values of kcat/Km for the H257Y/L303T (YT) mutant for the hydrolysis of GB, GD, and GF were determined to be 2 106, 5 105, and 8 105 M1 s1, respectively. The YT mutant is the most proficient enzyme reported thus far for the detoxification of G-type nerve agents. These results support a combinatorial strategy of rational design and directed evolution as a powerful tool for the discovery of more efficient enzymes for the detoxification of organophosphate nerve agents.

Journal reference: Biochemistry

Provided by American Chemical Society

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New substances 15,000 times more effective in destroying chemical warfare agents

Public release date: 26-Jul-2012 [ | E-mail | Share ]

Contact: Natasha Pinol npinol@aaas.org 202-326-6440 American Association for the Advancement of Science

When Brian White was a child, his kindergarten teacher wrote in his student record that he would only talk to the other children if the topic was science. Throughout his childhood, White's fascination with science led him to take batteries apart, blow things up, and to build radios and computer components.

Now an associate professor in the biology department at the University of Massachusetts, Boston, White is the winner of the Science Prize for Inquiry-Based Instruction (IBI). He won the award for his creation of Aipotu, a computer-simulated world in which students apply the tools of genetics, biochemistry, molecular biology and evolution to develop an understanding of the formation of color in a flower.

"What I'm trying to do is give people the tools to play around," says White, who explains that Aipotu is "utopia" backward. "What I've always liked about science is what you could do with what you learned."

Science's IBI Prize was developed to showcase outstanding materials, usable in a wide range of schools and settings, for teaching introductory science courses at the college level. The materials must be designed to encourage students' natural curiosity about how the world works, rather than to deliver facts and principles about what scientists have already discovered. Organized as one free-standing "module," the materials should offer real understanding of the nature of science, as well as providing an experience in generating and evaluating scientific evidence. Each month, Science publishes an essay by a recipient of the award, which explains the winning project. The essay about Aipotu will be published on July 27.

"We're trying to advance science education," says Bruce Alberts, editor-in-chief of Science. "This competition provides much-needed recognition to innovators in the field whose efforts promise significant benefits for students and for science literacy in general. The publication in Science of an article on each laboratory module will help guide educators around the globe to valuable free resources that might otherwise be missed."

After many hours of experiments in his parents' basement, White went on to MIT for his undergraduate work. Many of his classes were lectures, but by his junior year, he was able to take a class that had him in the lab all afternoon every day.

"I cooked up many harebrained experiments," White says. "In the lab, you learn problem-solving. Most of the time, what you attempt doesn't work, so you have to figure out why."

Throughout his education, White had some wonderful teaching experiences, he says, including at a science camp in Woods Hole, Massachusetts, where one of his students built a pinball machine that kept score. White said demonstrating the machine to the student's parents was an amazing moment, one of many that White had early on that drew him into education.

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Science magazine prize goes to virtual world where undergrads explore DNA

01.08.2012 - (idw) Goethe-Universitt Frankfurt am Main

Ivan Dikic will receive the William C. Rose Award 2013 FRANKFURT. Prof. Ivan Dikic, Head of the Institute of Biochemistry II and Director of the Buchmann Institute of Molecular Life Sciences at the Goethe University Frankfurt, was awarded with the William C. Rose Award 2013, as announced today by the American Society for Biochemistry and Molecular Biology.

With this Award, the American Society for Biochemistry and Molecular Biology recognizes outstanding contributions of Ivan Dikic to biochemical and molecular biological research and in particular his pioneering work in understanding the Ubiquitin Code that regulates multiple biological processes. The Award consists of a plaque and 3.000 US$ and will the awarded at the Annual Meeting in Spring, 2013, where Prof. DIkic will be invited to present his research.

Ivan Dikic has been working at the Medical Faculty of the Goethe University in Frankfurt since 2002. More then 10 years ago, he started to concentrate his work on the Ubiquitin Research. Prof. Dikic showed that Ubiquitin acts as a multivalent cellular signal recognized by an expanding number of binding proteins that in turn translate this molecular signal into appropriate cellular phenotypes. His group have identified several novel Ubiquitin binding domains and used structural and functional studies to demonstrate their roles in the regulation of DNA repair, inflammation, receptor endocytosis, and proteasomal degradation. Despite their biological relevance, modern-day tools to study Ub chains in their physiological environment remain rudimentary and mainly focus on the biochemical characterization of chains, substrates or ubiquitin-binding domains (UBDs). Lately, Ivan Dikics group described the development and in vivo application of highly versatile chain-specific Ub sensors.

Informations: Prof. Ivan Dikic, Institut fr Biochemie II and Buchmann Institute for Molecular Lifesciences, Campus Niederrad, Tel.: (069) 6301-5652; ivan.dikic@biochem2.de function fbs_click() {u=location.href;t=document.title;window.open('http://www.facebook.com/sharer.php?u='+encodeURIComponent(u)+'&t='+encodeURIComponent(t),'sharer','toolbar=0,status=0,width=626,height=436');return false;} html .fb_share_link { padding:2px 0 0 20px; height:16px; background:url(http://static.ak.facebook.com/images/share/facebook_share_icon.gif?6:26981) no-repeat top left; } Share on Facebook Weitere Informationen: http://www2.uni-frankfurt.de/42409151/038

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American Society for Biochemistry and Molecular Biology honors outstanding Scientists

Mariam Sattar has fasted for the 30 days of Ramadan every year since she was 7. It is a special time, a time when she feels closer not only to God, but to the millions of fellow believers around the world as they celebrate the most important holiday of their faith.

This year, however, the 22-year-old is four months pregnant. And despite the counsel of her gynecologist and the worries of her husband, the bubbly University of Houston biochemistry graduate wants to fast for as many days as she can during Ramadan, which begins Friday.

"There's this extra spiritual upliftment," Sattar said. "Any other day if you tell me to fast when I'm pregnant, I'm going to say, 'Oh my gosh, no thank you, I can't do that.' But when Ramadan comes by it's like, 'Of course, why wouldn't I?'"

Sattar is far from an outlier. Though most Muslim scholars agree that Islam exempts pregnant and breast-feeding women from fasting during Ramadan - which prohibits eating and drinking from sunrise to sunset - many still do.

Sattar's gynecologist. Dr. Dipika Ambani, said she sees about three pregnant Muslims a day in her Houston practice and most choose to fast, though she urges them not to. On a recent day this week, for instance, she counseled five.

"Two of them said they were going to fast no matter what," Ambani said. "Three of them asked my opinion, and when I told them it wasn't a good idea, they were kind of sad. I didn't know from their faces whether they were going to do it or not."

Likewise, Ambani told Sattar it's unwise. The young mother listened, then went home and did her own research online, decided she could re-hydrate sufficiently and boost her calories after dusk and before dawn, and was ready to take the plunge.

"You become this whole different person during Ramadan," she explained.

Five pillars of Islam

Sattar embodies, perhaps, the conflict some American Muslims feel during this annual period of reflection and worship. They lead modern lives and are highly educated and financially well off, but also deeply serious about their faith.

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Ramadan fasting poses quandary for mothers-to-be

National Autonomous University of Mexico uses dynamic light scattering for allosteric transition characterization

Using the Zetasizer V dynamic light scattering (DLS) system from Malvern Instruments, Professor Mario L. Calcagno and his team at the Biochemistry Department of the Faculty of Medicine, Universidad Nacional Autnoma de Mxico (UNAM, the National Autonomous University of Mexico) have been able to distinguish allosteric transition [structural rearrangements] in a single E. coli protein. Characterizing protein allostery is challenging because of its sensitivity to experimental conditions, however, a quantitative description of allosteric transition is important in understanding and controlling metabolic and other biochemical processes.

We use the Zetasizer V to characterize the size of proteins and how they interact to produce multimeric forms or even supramolecular arrangements of the protein such as viral capsids [shells], said Dr Ismael Bustos-Jaimes, from Laboratory of Physical Chemistry and Protein Engineering at UNAM commented The Zetasizer V allows us to work with sizes in the range of 1 nm to 500 nm and follow each assembly and stability parameter, such as pH, temperature and ionic strength, guiding us to the optimal production conditions for these virus-like particles.

The sensitivity of the Zetasizer V has additionally allowed my colleague, Prof Calcagno, to analyze allosteric transitions explained Dr Bustos-Jaimes. The size of the hexameric glucosamine-6-phosphate deaminase protein from E. coli changes its shape to a more compact form upon allosteric-activator binding, and this change can be measured.

The Zetasizer V software is user-friendly and in addition to measuring particle size it delivers information about the quality of sample preparation. This is very important when you work with molecules which are prone to uncontrolled aggregation, said Dr Bustos-Jaimes.

The UNAM team studies allosteric transitions and the assembly of virus-like particles (VLPs) for use in diagnostics and disease control. VLPs are biological nanoparticles that resemble natural viruses but contain no genetic material. As non-infective agents, they are suitable for use in the analysis of viral infection mechanisms, vaccine production, tissue-specific drug delivery and as biological nanomaterials.

The Zetasizer V is part of a range of Zetasizer dynamic light scattering systems from Malvern Instruments. For more information, visit http://www.malvern.com/zetasizer

About Malvern Instruments Malvern Instruments is a market leader in measuring performance controlling material properties. These include particle size, particle shape, zeta potential, molecular weight, size and conformation, rheological properties and chemical identification. Malvern delivers the systems, support and expertise that ensure the analytical integrity and productivity needed to drive research, development and manufacturing.

Malverns measurement solutions for scientists, technologists and engineers advance continually through customer collaboration. Complementary materials characterization systems deliver inter-related measurements that reflect the complexities of particulates and disperse systems, nanomaterials and macromolecules. Combining intelligently implemented technologies with in-depth industry applications knowledge and support, Malvern provides customers with the competitive advantage they demand.

Headquartered in Malvern, UK, Malvern Instruments has subsidiary organizations in all major European markets, North America, China, Japan and Korea, a joint venture in India, a global distributor network and applications laboratories around the world. For more information, visit http://www.malvern.com

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Zetasizer µV Used In Measuring Protein Structural Transition

Public release date: 24-Jul-2012 [ | E-mail | Share ]

Contact: Angela Hopp 240-283-6614 American Society for Biochemistry and Molecular Biology

Human defensins, aptly named antimicrobial peptides, are made in immune system cells and epithelial cells (such as skin cells and cells that line the gut). One of these peptides, human neutrophil peptide 1, under certain circumstances hinders HIV infection, but exactly how it works remains unclear.

HIV entry into mature T-helper cells (cells essential to the immune system) proceeds by attachment of the virus to specific targets on T-helper cells, uptake of the virus, fusion of its envelope with the cell membranes, and release of the virus into the cells. In a forthcoming Journal of Biological Chemistry Paper of the Week, Gregory Melikyan at Emory University and colleagues investigated the ability of human neutrophil peptide 1 to impede each step of this process.

Using model cell lines, Melikyan's group showed that human neutrophil peptide 1 effectively prevented HIV entry into cells in multiple ways. First, human neutrophil peptide 1 reduced the number of specific targets on the cells available for HIV attachment. Second, this defensin also bound to specific targets on both the HIV envelope and the cells, preventing early and late stages of HIV-cell fusion. Finally, human neutrophil peptide 1 prevented HIV uptake into the cells without compromising the general ability of the cells to engulf other molecules.

While human neutrophil peptide 1 hinders HIV entry into cells under these lab conditions, it does not do so as effectively in the presence of serum -- meaning that it may not be as successful at blocking HIV in our bodies. But Melikyan's team showed that human neutrophil peptide 1 remained attached to its specific targets in the presence of serum, despite its reduced efficacy. Their work suggests that the structure of human neutrophil peptide 1 is important for its anti-HIV activity, and they propose that serum may interfere with the ability of this defensin to form complexes, reducing its ability to block HIV.

"Our work provides new insights into the ability of defensins to recognize and neutralize diverse pathogens, including HIV," Melikyan says. This research reveals that human neutrophil peptide 1 can bind various viral and cellular targets and that a previously unappreciated feature is essential for its anti-HIV activity, possibly its propensity to form large complexes, Melikyan explains.

The team's findings suggest a new avenue of research for combatting HIV and viruses that infiltrate cells in a similar manner.

###

From the article: "Multifaceted mechanisms of HIV-1 entry inhibition by human alpha-defensin" by Lusine H. Demirkhanyan, Mariana Marin, Sergi Padilla-Parra, Changyou Zhan, Kosuke Miyauchi, Maikha Jean-Baptiste, Gennadiy Novitskiy, Wuyuan Lu, and Gregory B. Melikyan (to be published in the Aug. 17 issue of the Journal of Biological Chemistry and currently online as a Paper in Press at http://www.jbc.org/content/early/2012/06/25/jbc.M112.375949.full.pdf)

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Under the right conditions, peptide blocks HIV infection at multiple points along the way

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Author and scientist Dee Takemoto edits her latest book in her Aptos studio. takemoto taught biochemistry for 32 years at Kansas State University and recently published a book detailing the corn syrup/obesity relationship.

APTOS -- To Dee Takemoto, retiring from teaching biochemistry for 32 years at Kansas State has meant tackling books she's been meaning to write.

"I haven't really wanted to slow down yet," the 63-year-old Aptos resident said.

Takemoto published "Gaining Weight? High Fructose Corn Syrup and Obesity" in January, just wrapped up her first novel [science fiction, of course], and is finishing up a book about genetics and obesity. In addition to writing, Takemoto edits science journals from China, Korea and Japan.

While Takemoto used to study primarily diabetic retinopathy, she said she became interested in studying obesity after more and more of her students at Kansas State seemed overweight. She challenged them to omit corn syrup from their diets, which Takemoto said led them to lose an average of 40 pounds per person.

Takemoto said she decided to further study this connection in her book.

"I have a number of people who call me and say it's an easy diet to be on because you don't have to give up your favorite stuff," Takemoto said. "I'm just really committed to people losing weight."

Takemoto began her career in health and sciences at USC, where she earned a doctorate in molecular biology. She and her husband Larry Takemoto [he received a doctorate in biology from UCLA] were offered tenure-track positions teaching at Kansas State.

Moving to Manhattan Center, Kansas, took a bit of adjusting, said Larry Takemoto.

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Dee Takemoto, Santa Cruz County Stories: Former professor stays busy in retirement as an author

The Irish Times - Tuesday, July 17, 2012

DOMINIC COYLE

Q&A:Last June I completed a biochemistry degree in Dublin and moved to England to start graduate medicine. When I started to look for ways to finance the degree, I hit about a 100 brick walls. My parents are not in a position to fund me.

I went to the local branch of the bank, where I have always banked, and was told there were no such loans for graduate students but to apply for a student loan with a reduced rate APR. Although a four-year course, I was told to apply for the funds for year one and to review it in year two.

The initial 11,000 interest- only facility proved to be too little. When I went to top up my loan to 20,000, the student officer became involved. She was surprised that a loan for the four years wasnt put in place, but when I tried to get a four-year plan in place for a loan of 80,000, I was told I would need to put up front some sort of security. They released the extra money for first year but are looking for that security before releasing more funds and that they will probably want me to start full repayments on the loan.

The bank said they could look at topping up my parents mortgage on an interest-only basis and they could give me that money, but their mortgage isnt with the AIB. I cannot afford to make full repayments either until I am a qualified doctor in 2015. Essentially, I am making the interest repayments from the loan money.

I need to find a solution as my funds will dry up in August and if I cannot get the financial support I will have to quit college to get a job and pay back this 20,000 the bank has already given me.

Ms S.OB., England

There are two issues here. First, you are in an incredibly difficult position because of the rules covering grant aid across national boundaries; second, your bank appears to have been, at best, unhelpful in the mixed messages it has given on funding options, especially in your original application for financial support.

Desperate to fund your course, you have embarked without a clear four-year funding plan. I dont have a clear answer for you and am running your query as much in the hope that someone may provide an answer to your plight as anything else. If colleges are accepting cross-border students, I would assume there must be some funding options available as not everyone is in a position to fund 80,000 or more from their own, or their parents, resources.

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Bank won't fund my medical course in England

Eagle photo by Dave McDermand Workers carefully line up placement Thursday for a super-conducting magnet that arrived on Texas A&Ms West Campus.

A 100-ton crane sat outside Texas A&M Universitys biochemistry and biophysics building Thursday not an uncommon site for the construction-heavy campus.

But the cranes presence had nothing to do with raising another new building. Instead, it was there to lift a four-metric-ton, 800 megahertz Nuclear Magnetic Resonance spectrometer through an opening in the roof of the building.

The installation of the NMR, which will be complete in two to three months, puts A&M on par with other top national research institutions, Dr. Gregory Reinhart, head of the biochemistry and biophysics department, said.

NMR spectroscopy functions similar to the way an MRI takes images of the body, Reinhart said. NMR was developed first, and expanded into the imaging technique known as MRI. NMR, however, allows for higher precision for molecular information.

In NMR, we dont look at large objects, rather we look at individual molecules, like proteins and nucleic acids, Tatyana Igumenova, assistant professor and director of the NMR facility, said. This kind of instrument will allow us to determine the structure and dynamics of those molecules.

The NMR will be extremely powerful for research in drug design, Igumenova said.

You can identify potential drug candidates and use an NMR to determine where exactly they bind to the protein or enzyme, and what kind of effect they have on the structure and dynamics, Igumenova said.

With these capabilities, researchers will be able to design improved inhibitors to prevent the spread of disease.

The NMR, along with the upgrade and relocation of two other instruments to the NMR facility, cost a total of $2.7 million. The NMR itself cost more than $2 million, Reinhart said.

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Installation of new spectrometer gets under way on A&M campus

Public release date: 13-Jul-2012 [ | E-mail | Share ]

Contact: Kathleen Phillips ka-phillips@tamu.edu 979-845-2872 Texas A&M AgriLife Communications

COLLEGE STATION Top-notch molecular research swung into gear at Texas A&M University this week literally.

A crane lowered a high-field 800 megahertz Nuclear Magnetic Resonance spectrometer through an opening in the roof of a biochemistry and biophysics building Wednesday, putting the university on par with leading U.S. research institutions, according to Dr. Gregory Reinhart, department head.

The German-made instrument, which was flown on a cargo plane accompanied by an engineer and transported to the Texas A&M campus on a special truck, is expected to be fully operational by the first of September.

The Nuclear Magnetic Resonance technique, commonly called NMR, is the forerunner of the more widely known MRI. Reinhart explained that an MRI makes images of human tissue for medical diagnostics, but NMR makes images at the molecular level for scientific exploration.

"This is a major step forward in the capability of the university in the general area of structural biology," said Reinhart, whose department collaborated with Texas AgriLife Research, a part of the Texas A&M System, to obtain the equipment.

The equipment will benefit researchers from across Texas A&M, officials noted.

"We are excited to partner with Texas A&M University to bring this powerful instrument to campus," said Dr. Craig Nessler, AgriLife Research director. "It is critical that we find ways to collaboratively provide such state of the art equipment to our scientists to maintain our research competitiveness."

Structural biology means looking at macromolecules which consist of hundreds or thousands of atoms and then deducing the way these are built and how they move, Reinhart said. Knowing how the molecules work helps scientists create solutions for a variety of needs.

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Science goes through the roof

The bacterium Escherichia coli (E. coli) has a rudimentary molecular "memory" that allows it to swim toward the richest sources of food. MU biochemistry professor Gerald Hazelbauer's continuing discoveries about how bacteria do this could shed light on human and animal sensory, memory and response systems.

"My doctoral work was with Julius Adler, the first scientist to study the molecules behind bacterial behavior. His work led to the discovery that bacteria have a molecular 'memory' system that allows them to 'remember' the past, compare it to the present and thus move toward the area that is most favorable," Hazelbauer said. "When I began my work as a researcher in the late 1960s, studying bacterial behavior was a curiosity and its significance unclear. Now, decades later, the research done by my group and others has grown into a body of knowledge about the fundamental processes used by all living things to recognize, remember and respond to changes in their environments."

The National Institute of General Medical Sciences (NIGMS) recently recognized and rewarded Hazelbauer's scientific contributions by granting him a "Method to Extend Research in Time" (MERIT) Award. The award, which is worth at least $5.5 million over 10 years, will allow him to continue his research without re-applying for funding. Hazelbauer joins only 11 other MU researchers who have received the MERIT award, including his wife, Linda Randall, who is also a biochemistry professor.

MERIT awards are intended to foster creativity and allow researchers to take more time to develop new techniques. The awards are given only to scientists who have proven themselves by succeeding in at least 10 years of previous NIGMS-funded research and who seem likely to continue making valuable contributions to their field.

Hazelbauer is professor and chair/director of biochemistry, a department/division jointly administered by the University of Missouri's School of Medicine and College of Agriculture, Food and Natural Resources. Linda Randall is the Wurdack Professor of Biological Chemistry in that unit.

Provided by University of Missouri-Columbia

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Like humans bacteria remember (if only for 4 seconds), says researcher