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The 2008 Carl Brändén Award

Howard Schachman, Ph.D.
University of California, Berkeley

The Carl Brändén Award, sponsored by Rigaku Corporation, is given to an outstanding protein scientist who has also made exceptional contributions in the areas of education and/or service to the science.

The 2008 award will be presented to Dr. Howard Schachman (University of California, Berkeley), on Saturday, July 19, 2008 for his major contributions to protein science and for his exceptional contribution to both service and education. Dr. Schachman has pioneered research on the ultracentrifuge and proteins such as aspartate transcarbamylase. More than 150 students and postdoctoral fellows have received training in his laboratory. He has served as President of both ASBMB and FASEB, and as the NIH Ombudsman in the Basic Sciences. Through his articles, speeches and testimony before Committees of the United States Congress and government agencies, Dr. Schachman also has made crucial contributions toward the formulation of policies aimed at preserving academic freedom and fostering the responsible conduct of research.

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The 2008 Dorothy Crowfoot Hodgkin Award

Douglas Rees, Ph.D.
California Institute of Technology

The Dorothy Crowfoot Hodgkin Award, sponsored by Genentech, is granted in recognition of exceptional contributions in protein science, which profoundly influence our understanding of biology.

The 2008 Award will be presented to Dr. Douglas Rees (California Institute of Technology) on Saturday, July 19, 2008 for his fundamental contributions to the understanding of the structural biology of metalloproteins and membrane proteins, most notably by his analyses of the nitrogenase molybdenum-iron (MoFe-) protein that established the unprecedented structure of the FeMo-cofactor providing the active site for biological nitrogen fixation.  Dr. Rees’ work also resulted in:   the first structure determination of a physiologically gated ion channel, the mechanosensitive channel of large conductance (MscL) from Mycobacterium tuberculosis; and the first structure determination of an intact and fully ordered member of the widespread family of ABC transporters, the E. coli importer BtuCD for vitamin B12. (Solving the structure of vitamin B12 itself, many years ago, happens to be one of the main accomplishments of Dorothy Crowfoot Hodgkin.)

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The 2008 Stein and Moore Award

Susan Lindquist, Ph.D.
Whitehead Institute for Biomedical Research

The Stein and Moore Award, sponsored by The Merck Company Foundation, is named for Nobel Laureates Dr. William Stein and Dr. Stanford Moore.  The award venerates their contribution to understanding the connection between chemical structure and catalytic activity of the active center of the ribonuclease molecule. 

The 2008 award will be presented to Dr. Susan Lindquist (Whitehead Institute for Biomedical Research) on Tuesday, July 22, 2008 for her groundbreaking discoveries in understanding the wide array of biological processes governed by protein folding.  Dr. Lindquist has resolved a variety of difficult problems, ranging from delineating cellular responses to stress, the role of protein misfolding in genetics and disease, to uncovering genetic variation in evolution. Her pioneering studies of the heat shock response led to her groundbreaking work on eukaryotic gene expression and her subsequent contribution to establishing the function of the stress response and of several of its individual proteins. Dr. Lindquist’s work on prions provided the molecular framework for an extraordinary new form of protein based inheritance. Taken together, her work on chaperones and prions has provided entirely new concepts for how organisms exploit hidden genetic variation for phenotypic plasticity and the evolution of new traits. Her overall body of work reveals the large variety of unexpected effects that changes in protein folding have on biological systems.

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The 2008 Hans Neurath Award

Robert Stroud, Ph.D.
University of California, San Francisco

The Hans Neurath Award, sponsored by the Hans Neurath Foundation, recognizes an individual who has made a recent contribution of unusual merit to basic research in the field of protein science, including but not restricted to the chemistry, design, folding, structure, or biological function of proteins.  

The 2008 award will be presented to Dr. Robert Stroud (University of California, San Francisco) on Saturday, July 19, 2008 for his significant contributions to the understanding of structure function relationships in enzymes and membrane proteins.  Dr. Stroud’s work has focused on the molecular levels of cellular signaling and communication across cell membranes as well as the macromolecular encoding of specificity and affinity at protein/protein and protein/ligand interfaces.  He has determined the high resolution three dimensional structures of numerous proteins of different classes and used these structures to define biological, biochemical, and cellular function—as templates for drug design.  Dr. Stroud’s seminal contribution of defining the mechanism of zymogen activation by demonstrating structurally that the catalytic site becomes rearranged is now taught in any undergraduate biochemistry course.  Recent studies on enzyme mechanism focus on:  thymidylate synthase with an emphasis on designing better drugs; and polyketide synthases with an emphasis on exploring biotechnological opportunities of producing new polyketide compounds.  Another recent highlight includes the structure of the EPO-EPO receptor complex, which shows a 2:1 stoichiometry of binding for the cytokine and provides a major contribution to our understanding of cell surface signaling.

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The 2008 Christian B. Anfinsen Award

Carol Robinson, Ph.D.
University of Cambridge

The Christian B. Anfinsen Award, sponsored by The Aviv Family Foundation, recognizes significant technical achievements in the field of protein science. 

The 2008 award will be presented to Dr. Carol Robinson (University of Cambridge) on Saturday, July 19, 2008 for her outstanding pioneering scientific contributions in the fields of mass spectrometry and structural biology.  In her research pursuits, Dr. Robinson has driven the continual development of novel mass spectrometry approaches and instrumentation that are used in laboratories around the world.  Her early work provided insights into the folding of protein substrates within the cavity of GroEL.  After contributing to the development of a prototype electrospray time-of-flight mass spectrometer that substantially extended the mass/charge range, she designed a more sophisticated machine, a high mass quadrupole time-of-flight mass spectrometer that has been produced and installed in many laboratories around the world.  Using this technology, Dr. Robinson demonstrated that macromolecular particles with masses in excess of 2MDa can transverse the mass spectrometer in an intact state, permitting the recording of their mass spectra.  In her exploration of the extent to which solution phase complexes resemble those studied in the gas phase of the mass spectrometer, Dr. Robinson used ion mobility measurements of protein complexes to show that the 11-mer protein rings formed by the RNA binding protein TRAP could not only be retained in the gas phase but their stability could be altered by the addition of cofactors.  This finding presents an unprecedented opportunity to capture in the mass spectrometer transient species in dynamic equilibrium in solution, thereby facilitating insights into structures proposed to be the causative agent in amyloid diseases.

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The Emil 2008 Thomas Kaiser Award

JoAnne Stubbe, Ph.D
Massachusetts Institute of Technology

The Emil Thomas Kaiser Award, sponsored by The Protein Society, recognizes a recent, highly significant contribution in applying chemistry to the study of proteins.

The 2008 award will be presented to Dr. JoAnne Stubbe (Massachusetts Institute of Technology) for her outstanding contributions to the understanding of the involvement of cell enzymes in the production and breakdown of DNA.  Dr. Stubbe has demonstrated that although there are three classes of ribonucleotide reductases that use different active site chemical species to initiate their reactions, they all perform an initial abstraction of hydrogen from the C-3 position of the sugar substrate.  This aspect of the ribonucleotide reductase mechanism can be found in almost all modern Biochemistry textbooks.  Another conceptual breakthrough to Dr. Stubbe’s credit is that of finding the production of a thiyl radical in the ribonucleotide reductase from Lactobacillus leichmanni.  Also, Dr. Stubbe has designed a number of compounds that are analogs of the natural substrates for these enzymes and that have been found to behave as potent inhibitors. One of these compounds has proven effective in the treatment of pancreatic and possibly other cancers.

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The Emil 2007 Thomas Kaiser Award

Michael Marletta, Ph.D
University of California – Berkeley

The Emil Thomas Kaiser Award, sponsored by The Protein Society, recognizes a recent, highly significant contribution in applying chemistry to the study of proteins. 

The 2007 and 2008 awards will be presented on Tuesday, July 22, 2008.  The 2007 award will be presented to Dr. Michael Marletta (University of California, Berkeley) for his significant contributions to the field of nitric oxide (NO) biochemistry.  His work has greatly enhanced the understanding of the molecular basis for nitric oxide synthesis and signaling in mammalian cells.  The emergence of NO as a signaling agent came from independent research in the laboratories of Moncada, Hibbs and Marletta among others. In 1985, Dr. Marletta demonstrated that mouse macrophages produced nitrite and nitrate. This in turn led to the discovery of NO in mammals.  Before this time, NO biosynthesis was thought to be restricted to bacteria engaged in nitrification reactions.  The idea that higher organisms could produce this unstable, toxic diatomic free radical was considered extremely unlikely.

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The 2008 Irving Sigal Young Investigator Award

Jamie Doudna Cate, Ph.D
University of California, Berkeley

The Irving Sigal Young Investigator Award, sponsored by Merck Research Laboratories, recognizes a significant contribution to the study of proteins by a scientist who is in the early stages of an independent career and, generally, not more than 40 years of age at the time of the award. 

The 2008 award will be presented to Dr. Jamie Doudna Cate (University of California, Berkeley) on Tuesday, July 22, 2008 for his outstanding pioneering scientific contributions to the field of structural biology, particularly to our understanding of the structures of RNA and ribosomes.  As a postdoctoral student, Dr. Cate solved the crystal structure of the entire 70S ribosome at 5.5 Å resolution, which at 2.5 MDaltons remains the largest asymmetric structure ever solved by X-ray crystallography.  His research as an independent investigator has continued at the cutting edge of RNA and ribosome research, focusing on the E. coli ribosome.  Last year, Dr. Cate’s group published a paper in Science describing the 3.5 Å structure of two conformational states of the E. coli 70S ribosome—the first all-atom structures of the complete ribosome.

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