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We are now accepting nominations for the 2019 Protein Society Awards.  Submissions are due November 15, 2018. 

Learn more and submit your nomination.


The Protein Society announces its 2019 Call For Nominations. View the press release below.

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To learn more about the benefits of becoming a Protein Society member, including complimentary access to the Protein Science journal, please visit: https://www.proteinsociety.org/page/join-renew.


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The Protein Society is the leading international Society devoted to furthering research and development in protein science. Founded in 1986, the purpose of the Society is to provide international forums to facilitate communication, cooperation, and collaboration regarding all aspects of the study of proteins. In support of these goals, the Society publishes Protein Science, the premier journal in the field, hosts an annual international symposium, and facilitates the education of early-career protein scientists across all lines of discipline. The Protein Society members represent a wide spectrum of academic, industry, governmental, and non-profit institutions from more than 50 countries around the world. Media inquiries can be directed to Raluca Cadar, Executive Director, at 844.377.6834.


The Protein Society announces its 2018 Award Recipients. To view the official press release, click here.  

Protein Society Awards

TPS 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

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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 Winners

2017 - Billy Hudson
2016 - Gary Pielak
2015 - C. Robert Matthews

2014 - Stephen White
2013 - Sheena Radford
2012 - Helen Berman
2011 - Michael Summers
2010 - Nobuhiro Go
2009 - Bruce Alberts
2008 - Howard Schachman
2007 - Lubert Stryer

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

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Established in 1996 and named for Nobel laureate Christain Boehmer Anfinsen, whose research on the structure and function of enzyme proteins contributed to the general acceptance of the “thermodynamic hypothesis,” The Christian B. Anfinsen Award recognizes significant technological achievements and/or methodological advancements in protein research.

Specific Requirement: Technological achievement or significant methodological advances.

Previous Award Winners

2017 - Lewis Kay
2016 - Andreas Pluckthun
2015 - Sachdev Sidhu
2014 - Robert Tycko
2013 - Tom Albert
2010 - Yoshinori Fujiyoshi
2009 - Wayne Hubbell
2008 - Carol Robinson
2007 - Carl Frieden
2006 - John R. Yates, III
2005 - Matthias Mann
2004 - Meir Wilchek
2003 - Ada Yonath
2002 - Roger Tsien
2001 - Martin Karplus
2000 - Stephen Benkovic
1999 - Alan Fersht
1998 - James Wells
1997 - Wayne Hendrickson
1996 - Donald Hunt

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

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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
2016 - Rachel Klevit
2015 - Eva Nogales
2014 - Judith Frydman

2013 - Christopher Hill and Cynthia Wolberger
2012 - Mark Lemmon
2011 - Brenda Schulman and Wei Yang
2010 - Lila Gierasch
2009 - Janet Thornton
2008 - Douglas Rees
2007 - Leemor Joshua-Tor

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

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In 2002, The Protein Society established The Emil Thomas Kaiser Award. Dr. Kaiser’s highly original research, including the profoundly significant discovery of the necessity amphiphilic helices to biological life, can be said to have introduced a new field of chemistry. In this tradition, The Emil Thomas Kaiser Award recognizes a recent, highly significant contribution in applying chemistry to the study of proteins. 

To make a donation in support of the Kaiser Award Endowment, please visit this webpage.

Specific Requirement: Application of chemistry to the study of proteins.

Previous Award Winners

2017- Thomas Muir
2016 - Charles Craik
2015 - Anna Mapp
2014 - Carol Fierke
2013 - Wilfred van der Donk
2010 - Suzanne Walker
2009 - Donald Hilvert
2008 - JoAnne Stubbe
2007 - Michael Marletta
2006 - Barbara Imperiali

Previous recipients, sponsored by SynPep Corporation, include:

2005 - Ronald Raines
2004 - Homme Hellinga
2003 - Michael Hecht
2002 - Steve Kent

Michael Rosen, 2018
Emil Thomas Kaiser Award Winner

(University of Texas SW Medical School) 

The 2018 recipient is Professor Michael Rosen. Dr. Rosen has been a leader in deciphering how macromolecular phase separation organizes eukaryotic cells through formation of biomolecular condensates, compartments that concentrate proteins and RNA without a surrounding membrane. Of greatest current impact is his seminal work on liquid-liquid phase separation in cells and how the resulting membrane-less organelles participate in fundamental cellular physiology. His group showed that diverse multivalent molecules, including natural and engineered multidomain proteins, intrinsically disordered proteins and nucleic acids, undergo phase separation in vitro and in cells, forming distinct structures with unique functions. Further, they demonstrated how covalent modifications can control the formation and dissolution of condensates and provided initial models to explain condensate composition. Dr. Rosen’s work has important implications for protein chemistry, biophysics and cell biology, and for human diseases such as neurodegenertion and cancer.


Hans Neurath Award

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Hans Neurath played an integral role in the early life of the Society, as a founding member and later -at age 81- as founding editor of Protein Science. His contributions to the early success of the Society were surpassed only by his larger contributions to the field of biochemistry and our early understanding of proteins.

Reflective of his prolific contributions to the understanding of the physical chemistry of proteins, The Hans Neurath Award, sponsored by the Hans Neurath Foundation, seeks to honor individuals who have made a recent contribution of exceptional merit to basic protein research.

Specific Requirement: A recent contribution of unusual merit to basic protein science.

Previous Award Winners

2017 - Kazuhiro Nagata
2016 - H. Eric Xu
2015 - Marina Rodnina
2014 - James Hurley
2013 - Jennifer Doudna and Chuck Sanders
2012 - Charles Brooks
2010 - Wendell Lim
2009 - William Eaton
2008 - Robert Stroud
2007 - Robert Sauer
2006 - Christopher Dobson
2005 - Roderick MacKinnon
2004 - Carlos Bustamante
2003 - James Wells
2002 - Ad Bax
2001 - Arthur Horwich
2000 - Janet Thornton
1999 - Peter Kim
1998 - Ken Dill

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

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The Stein and Moore Award, named for Nobel laureates Dr. William Stein and Dr. Stanford Moore, venerates their contribution to understanding the connection between chemical structure and catalytic activity of the active center of the ribonuclease molecule. Established in 1986, the Stein and Moore Award is given to recognize eminent leaders in protein science who have made sustained high impact research contributions to the field.

Specific Requirement: Sustained, high-impact research contributions to the field.

Previous Award Winners

2017 - John Kuriyan
2016 - Jane Clarke
2015 - William DeGrado
2014 - Nikolaus Pfanner
2013 - Robert T. Sauer
2010 - Peter Wright
2009 - Peter Walter
2008 - Susan Lindquist
2007 - Paul Schimmel
2006 - Arthur Horwich and F. Ulrich Hartl
2005 - Avram Hershko and Alexander Varshavsky
2004 - Wolfgang Baumeister
2003 - Chris Dobson
2002 - Paul Sigler
2001 - Alan Fersht
2000 - Brian Matthews
1999 - Mo Cleland
1998 - David Davies
1997 - Mildred Cohn
1996 - David Eisenberg
1995 - Harold Scheraga
1994 - Michael Rossman
1993 - Walter Kauzmann
1992 - Robert Baldwin
1991 - Russell Doolittle
1990 - Kurt Wuthrich
1989 - Hans Neurath
1988 - Fred Richards
1987 - Emil Smith

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

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The Protein Science Young Investigator Award, formerly known as The Irving Sigal Young Investigator Award, recognizes a scientist in the first 8 years of an independent career who has made an important contribution to the study of proteins.*

*With allowances for familial leave or other exigent circumstance.

Specific Requirement: Within 8 years of starting an independent career.

Previous Award Winners

2017 - David Pagliarini
2016 - Benjamin Garcia
2015 - Nieng Yan
2014 - M. Madan Babu
2013 - Feng Shao
2010 - Charalampos Kalodimos
2009 - Virginia Cornish
2008 - Jamie H. Doudna Cate
2007 - Benjamin Cravatt, III
2006 - Vijay Pande
2005 - Thomas Muir
2004 - Erin OíShea and Jonathan Weissman
2003 - Yigong Shi
2002 - Carolyn Bertozzi
2001 - Kevan Shokat
2000 - David Baker
1999 - Jeffery Kelly
1998 - Nikola Pavletich
1997 - John Kuriyan
1996 - Michael Summers
1995 - Stuart Schreiber
1994 - Peter Kim
1993 - Ad Bax and Marius Clore
1992 - Peter Schultz
1991 - Carl Pabo
1990 - Rachel Klevit
1989 - William DeGrado

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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