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| Nominations are due annually by October 31. In 2018, we will present our awards at the 32nd Annual Symposium of The Protein Society in Boston, Massachusetts, July 9 - 12. ..
The Protein Society announces its 2018 Award Recipients. To view the official press release, click here. |
Protein Society AwardsTPS awards recognize excellence across the diverse disciplines that collectively advance our understanding of proteins; their structure, function, design, and application. The Awards honor researchers who have distinguished themselves with significant achievements in protein research and those who have made outstanding contributions in leadership, teaching, and service. TPS members submit nominations, which are awarded by Executive Council, and recipients are honored at the Annual Symposium.
Read about the Best Paper Winners here. |
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Carl Brändén Award
In the tradition of Carl Brändén, pioneer in structural biology, co-author of the seminal text Introduction to Protein Structure, and leader of the world-class synchrotron facility at Grenoble, the Carl Brändén Award, sponsored by Rigaku Corporation, honors an outstanding protein scientist who has also made exceptional contributions in the areas of education and/or service. Specific Requirement: Sustained, high-impact research contributions to the field. Previous Award Winners2017 - Billy Hudson |
Jane & Dave Richardson, 2018 Carl Brändén Award Winners(Duke University)The 2018 recipients of this award, Jane & Dave Richardson have been involved in many groundbreaking developments through the years, including solving two of the first 20 protein crystal structures (Staph nuclease & Cu,Zn superoxide dismutase); early work in what is now called structural bioinformatics: (beta bulges, Greek key folds, helix caps, etc.); developing the ribbon drawing, still widely used to represent 3D protein folds both on the page and in 3D graphics -- the hand-drawn TIM barrel ribbon schematic was Picture of the Day on Wikipedia Nov 19, 2009; pioneering early protein de novo design in the 1980s with Betabellin and Felix; pioneering interactive 3D macromolecular graphics for small personal computers with the Mage/kinemage system, first used as digital supplements at the launch of Protein Science, then for the Branden & Tooze textbook, and later online with KiNG; developing the method of all-atom contact analysis, which adds explicit hydrogen positions to analyze packing inside and between macromolecules. It diagnoses and helps correct local modeling problems in protein and RNA structures. They were also involved in developing and updating the MolProbity validation web service, now used by most crystallography labs, within the Phenix software system, at deposition to the worldwide Protein Data Bank, and in crystallography courses; and are currently developing new validation methods suitable in the 2.5-4Å resolution range, for crystallography and especially for modern cryoEM. |
Christian B. Anfinsen Award |
Yifan Cheng, 2018 Christian B. Anfinsen Award Winner(University of California, San Francisco)The recipient of this award in 2018 is Professor Yifan Cheng. Yifan is considered one of the world’s top few experts in high-resolution cryo-EM. He has been involved in various groundbreaking technological developments that greatly advanced single particle cryo-EM and its application in studying integral membrane proteins. He has also been involved in the structural studies of TRP channels. In particular, Dr. Cheng has been involved in the determinations of TRPV1 ion channel, the first atomic structure of an integral membrane protein determined by single particle cryo-EM, and the determination of the atomic structure of TRPV1 in lipid nanodisc, the first membrane protein atomic structure in a lipid bilayer by single particle cryo-EM. These studies had major impact on structural biology of membrane proteins, and methods developed in these studies are now widely used in structural studies of a broad range of integral membrane proteins. |
Dorothy Crowfoot Hodgkin Award
Dorothy Crowfoot Hodgkin was a founder of protein crystallography as well as a Nobel laureate. 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. Specific Requirement: Profound influence on our understanding of biology. Previous Award Winners
2017 - Juli Feigon and Manajit Hayer-Hartl |
Susan Marqusee, 2018 Dorothy Crowfoot Hodgkin Award Winner(University of California - Berkeley)The 2018 recipient is Professor Susan Marqusee. Dr. Marqusee, a biophysical chemist whose work focuses on protein folding and dynamics, is one of the world’s top experimental scientists in the field of protein folding. Her work has led to the most complete characterization of a protein energy landscape and provided a rigorous and unprecedented detailed analysis of the diffusion of a folding protein on this energy surface, validating in this manner the hierarchical model of protein folding. She is known for many contributions, including the first de novo design of a short peptide that folded into a specific structure (alpha helix), the application of novel hydrogen exchange methods to measure rare partially-structured conformers, and the mechanical manipulation of single-protein molecules. Her work has produced the most detailed view of the energy landscape of a protein. Her work impacts areas of biology ranging from deciphering the effects of genome variation to the mechanism of protein misfolding pathologies. |
Emil Thomas Kaiser Award |
Michael Rosen, 2018
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Hans Neurath Award |
David Baker, 2018 Hans Neurath Award winner(University of Washington)
In 2018, the Hans Neurath Awardee is Professor David Baker. Dr. Baker’s scientific achievements have put him at the forefront of many disciplines in computational protein science over the past decade. Some of these achievements have included: Advances in de novo protein design and protein structure prediction of thousands of proteins of unknown structure using Rosetta atomistic modeling and evolutionary couplings; atomistic refinement of x-ray crystallographic structures, which has been packaged in the most popular software suite for x-ray crystallography, PHENIX; and reproducible design of stable, atomically accurate, small proteins, which may be used as binders and inhibitors. These breakthroughs required many additional technical advances in modeling and experimental characterization, and they reduce to practice what was for many decades the holy grail of protein science: fundamental understanding of the determinants of protein structure and stability that leads to consistent predictive capabilities, including the ability to design protein shapes and functions as desired. |
Stein & Moore Award |
Raymond Stevens, 2018 Stein & Moore Award winner(University of Southern California)The 2018 recipient is Professor Raymond Stevens (University of Southern California). Dr. Stevens has pioneered the development of membrane protein structural biology technologies including nanoliter crystallization robotics, nanoliter imaging, micro-expression and screening of constructs, thermal stability analysis, and the fusion partner tool chest that led to the ground breaking seminal work on the structures and mechanistic understanding of the G protein-coupled receptor superfamily. His latest and quite possibly most impactful endeavor is to create the first atomic model of the human body that can be used for testing drugs without any risk to patients’ health. He founded six biotechnology companies focused on structure-based drug design and was involved in the development of several marketed drugs to treat a number of different human diseases. Dr. Stevens also founded two research institutes - iHuman Institute in Shanghai, China and Bridge Institute in Los Angeles, CA. |
Protein Science Young Investigator Award |
Brandon Ruotolo, 2018 Protein Science Young Investigator Award winner(University of Michigan)
The 2018 recipient is Professor Brandon Ruotolo (University of Michigan). Dr. Ruotolo, Associate Professor of Chemistry, has made continual and substantive contributions to our understanding of protein structure in the absence of bulk solvent, performing pioneering ion mobility-mass spectrometry measurements on model peptide, protein and multi-protein complex systems that have illustrated the level of conformational memory retained by biopolymers in the gas phase. Ruotolo is also responsible for the creation of new measurement technologies that have furthered our understanding of protein biophysics and structure. Most recently, Ruotolo has spearheaded the development of collision induced unfolding for the rapid analysis of protein complex structure and stability and demonstrated the utility of such experiments for applications ranging from conformationally-selective inhibitor screening to the characterization of biotherapeutics. |
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