Dr. Yang will be recognized for her numerous studies that led her to propose a widely accepted model of two metal ion catalysis for a large class of nucleic acid enzymes. In her work, Dr. Yang has used powerful crystallographic and biochemical methods to define molecular mechanisms of DNA repair, replication and recombination.

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The 2011 Stein and Moore Award
PeterGerhard Wagner, Ph.D.
Harvard Medical School

The Stein and Moore Award, sponsored by The Protein Society, 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 2011 award will be presented at the 25th Symposium to Dr. Gerhard Wagner (Harvard Medical School) for his innumerable seminal contributions to protein science and for shaping the protein NMR field’s current state.  Dr. Wagner’s contributions include the first observations of the dynamics of a protein and H-exchange by NMR experiments that stimulated the development of the field of protein dynamics.  He pioneered strategies for performing spectral assignments in BPTI and demonstrated the efficacy of NMR as a method to determine protein structures.  Subsequently, Dr. Wagner introduced the world to triple resonance experiments that are fundamental to contemporary protein structural studies.  Using these and other techniques, he has determined the structure of over 50 proteins.  Additionally, he has contributed to the understanding of many biological questions involving the control of gene expression, apoptosis and T-cell activation and their interrelationship.  His most recent accomplishment is the determination of the structure of the voltage dependent anion channel (VDAC), a membrane protein from the outer mitochondrial membrane.

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The 2010 Hans Neurath Award
Wendell A. Lim, Ph.D.
University of California, San Francisco - HHMI

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 2010 award will be presented to Dr. Wendell A. Lim (University of California, San Francisco – HHMI) on August 1, 2010 for his studies encompassing a variety of techniques for understanding protein function. Dr. Lim’s research has set the stage for a new future in biology, which will enable researchers to engineer new signaling systems with potential implications for medicine and other biological applications. He has made seminal contributions that are central to a deep molecular understanding of cellular signaling pathways as well as illuminating the molecular logic of signal-transduction networks. At present, Dr. Lim’s research is aimed at linking together multiple regulatory modules to create cells that will be able to polarize and migrate in response to novels sets of signals. Dr. Lim is considered to be one of the foremost scientists working on the molecular understanding of signal transduction systems, with a remarkable range of scientific abilities in areas such as structural analysis, biochemistry, cell biology and mathematical modeling of cellular processes.

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The 2011 Hans Neurath Award
Johannes Buchner, Ph.D.
Technische Universität München

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 2011 award will be presented at the 25th Symposium to Dr. Johannes Buchner (Technische Universität München) for his numerous important contributions to protein science, specifically in the context of protein folding and molecular chaperones.  His rigorous biophysical analysis of the molecular mechanisms of chaperone proteins have rendered many important contributions including:  a concept for the function of small Hsps in the cellular chaperone machinery; the unraveling of the conformational cycle of Hsp90 and the function of its co-chaperones; the identification and characterization of membrane-protection as a novel function for orphan heat shock protein Hsp12 in yeast; and the discovery of the quality control mechanism for antibody assembly in the cell, which is based on a folding switch in one conserved domain.  Dr. Buchner’s work goes beyond molecular chaperones:  he recently elucidated the mechanisms of the cellular quality control for antibody folding and assembly, revealing some unexpected traits; and he discovered a membrane protective stress protein in yeast.

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The 2011 Christian B. Anfinsen Award
D. Wayne Bolen, Ph.D.
University of Texas Medical Branch

The Christian B. Anfinsen Award, sponsored by The Aviv Family Foundation, recognizes significant technical achievements in the field of protein science. The 2011 award will be presented at the 25th Symposium  to Dr. D. Wayne Bolen (University of Texas Medical Branch) for resolving the long-standing question of how urea denatures proteins and how compatible osmolytes force folding.  Dr. Bolen’s research shows that the predominant osmolyte effect is on the unfolded state and is exerted primarily on the backbone common to all proteins.  His work provides essential insight into the underlying folding process whereby urea unfolds proteins by favoring solvent: co-solvent backbone interactions and, concomitantly, by disfavoring the native fold, whereas protecting osmolytes do the opposite.  Dr. Bolen’s studies have significantly contributed to protein biochemists’ understanding that the osmolyte effect is universal throughout all three kingdoms of life.

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The 2011 Emil Thomas Kaiser Award
Jeffery W. Kelly, Ph.D.
The Scripps Research Institute

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 2011 award will be presented at the 25th Symposium to Dr. Jeffery Kelly (The Scripps Research Institute) primarily for his ongoing contributions to our understanding of the chemical nature of amyloid formation and the application of this understanding in innovative ways to an amyloid disease as well as therapeutics design.  Dr. Kelly’s research has resulted in an unprecedented example of a rationally designed therapeutic based on the knowledge and application of protein science and chemistry to a medical problem:  at least one of the small molecule therapeutics designed and synthesized in the Kelly lab is shortly expected to be employed in the clinic as therapy for familial amyloid polyneuropathy, the disease caused by accumulation of transthyretin amyloid.   Dr. Kelly’s other important scientific contributions include:  his direct application of synthetic organic chemistry to the development of compounds that inhibit amyloid formation in the clinic; his fundamental contributions to the understanding of the role of particular secondary structures in the stabilization of protein structure; and most recently, his novel and wide-ranging thinking upon the physiological role of amyloid.

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The 2011 Irving Sigal Young Investigator Award
Shu-ou Shan, Ph.D.
California Institute of Technology

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 2011 award will be presented at the 25th Symposium to Dr. Shu-ou Shan (California Institute of Technology) for her pioneering mechanistic studies on the fidelity of substrate targeting during the process of protein localization by the signal recognition particle (SRP) system.  At the core of Dr. Shan’s research has been the development of conformationally sensitive probes that identify different intermediate states so that their interconversions and energetics can be characterized.  Not only has her research had a profound impact on our understanding of the SRP targeting cycle it has also utilized a multidisciplinary approach encompassing the disciplines of chemistry, biochemistry, structural biology, biophysics, and cell biology.

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