The Advanced Photon Source
a U.S. Department of Energy Office of Science User Facility

Four APS Users Garner 2020 Protein Society Awards

The Protein Society, the premier international society dedicated to supporting protein research, announces the winners of the 2020 Protein Society Awards, which will be conferred at the World Conference on Protein Science 2020 (WCPS2020) in Sapporo, Japan, July 6 - 10. Plenary talks from select award recipients will take place throughout the 4.5-day event. The winners' scientific accomplishments, highlighted here as described by their nominators, demonstrate their lasting impact on protein science.

Researchers who carry out biological studies at the Advanced Photon Source (APS) were awarded four of the seven awards for 2020. They are:

The Christian B. Anfinsen Award, sponsored by The Protein Society, recognizes technological achievement or significant methodological advances in the field of protein science. The recipient of this award in 2020 is Professor Stephen Sligar (University of Illinois at Urbana-Champaign). Dr. Sligar's academic career has featured the discovery, development, and use of chemical and biophysical tools to understand fundamental problems in protein biochemistry and biophysics. Of relevance to the Anfinsen Award is his development of nanodiscs, which are patches of lipid membrane stabilized by a "belt" of membrane scaffolding proteins. By using nanodiscs, signaling proteins and macromolecular complexes that rely on a membrane can be readily studied in a native bilayer that is solubilized in an aqueous environment. Dr. Sligar's commitment to wide dissemination of the nanodisc technology has led to its use by hundreds of laboratories, amplifying the impact of his advances and broadly benefitting the field of protein science. (Prof. Sligar is co-author on eight peer reviewed papers based upon research at the DuPont-Northwestern-Dow Collaborative Access Team and X-ray Science Division 12-BM x-ray beamlines at the APS.)

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 2020 recipient is Professor Catherine Drennan (Massachusetts Institute of Technology). Dr. Drennan has made enormous contributions by solving high-resolution structures of proteins and protein complexes that enhance our understanding of the biology of metalloproteins. Dorothy Crowfoot Hodgkin was famous for using X-ray crystallography to determine the structure of Vitamin B12, and Dr. Drennan has provided monumental insights into the structure and function of proteins that bind to B12. Dr. Drennan is known for going beyond single proteins and elucidating structures that illuminate entire pathways, capturing multiple snapshots of enzymes as they proceed through their reaction cycles. Among her many notable accomplishments, Dr. Drennan determined the first structure of the cobalamin-dependent ribonucleotide reductase, one of the three enzymes that catalyze the final step in production of deoxyribonucleotides in all organisms. Dr. Drennan's insights are solidly etched into textbooks and the fabric of our field. Drennan is also an outstanding and widely recognized educator and a tireless advocate for inclusion and equity in science. (Prof. Drenann is co-author on 54 peer reviewed papers based upon research at the Northeastern Collaborative Access Team x-ray beamlines at the APS.)

The Hans Neurath Award, sponsored by The Hans Neurath Foundation, honors individuals who have made a recent contribution of exceptional merit to basic protein research. In 2020, the Hans Neurath Awardee is Professor Martin Gruebele (University of Illinois at Urbana-Champaign). Dr. Gruebele is widely known for introducing the advanced technology of flash heating and ultrafast spectroscopy to study protein folding. His work showed that early stages of protein folding, including initial collapse and formation of secondary structures, can occur in microseconds. These advances allowed the first direct comparisons between folding rates determined experimentally and folding rates estimated from simulations. More recently, Dr. Gruebele showed that fast folding can be studied in live cells. His work established that in vivo folding, while following similar physicochemical rules as in vitro folding, is significantly modulated by the different cellular environments in different parts of the cell. Dr. Gruebele's work brings the highest level of experimental innovation, experimental precision, and conceptual rigor to protein biophysics. (Prof. Gruebele is co-author on four peer reviewed papers based upon research at the Biophysics Collaborative Access Team x-ray beamline at the APS. )

The Stein & Moore Award, sponsored by The Protein Society, is named for Nobel laureates Dr. William Stein and Dr. Stanford Moore. The award is given to recognize eminent leaders in protein science who have made sustained high impact research contributions to the field. The 2020 recipient is Professor James Bowie (University of California, Los Angeles). Dr. Bowie has shown great creativity and rigor in astoundingly diverse areas of protein science. His 1991 Science paper "A method to identify protein sequences that fold into a known three-dimensional structure" introduced the important idea of protein structure prediction by threading. In the area of membrane protein science, he has contributed novel methods to quantify protein stability, to measure protein-protein interactions in lipid bilayers, and to crystallize membrane proteins in bicelles. He showed that internal hydrogen bonds provide only marginal stabilization of membrane proteins and that membrane proteins can have high kinetic stability. In the area of synthetic biology, Dr. Bowie has developed in vitro systems that enable the continuous production of biofuels and other molecules in cell-free systems of enzymes with self-regenerating cofactors. Dr. Bowie has also been a dedicated and generous citizen of the scientific community, where he has served in important roles including as President of The Protein Society and co-founder of the Gordon Research Conference on Membrane Protein Folding (with Carl Brändén awardee Karen Fleming). ( Prof. Bowie is co-author on eight peer reviewed papers based upon research at the Northeastern Collaborative Access Team x-ray beamlines at the APS.)

The other three winners are:  The Carl Brändén Award to Karen Fleming (Johns Hopkins University). The Emil Thomas Kaiser Award to Professor Shuguang Zhang (Massachusetts Institute of Technology). The Protein Science Young Investigator Award to Mohammad Seyedsayamdost ( (Princeton University).

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 40 countries around the world.

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