Professor James Bowie receives the 2020 Stein and Moore Award in recognition of his protein science research and service to the scientific community.
The award is given annually by the Protein Society Society “to recognize eminent leaders in protein science who have made sustained high-impact research contributions to the field.”
In announcing the award, which will be conferred at the society’s annual symposium in July in Sapporo, Japan, the organization noted: “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).”
Bowie got hooked on proteins at an early age and never looked back. The obsession began as a high school student when he did a research project on blood clotting enzymes with Kenneth G. Mann at the Mayo Clinic in his hometown of Rochester, Minnesota. The research project won him a trip to the International Science and Engineering fair and a Westinghouse Award, experiences that further stimulated his interest in science.
He went on to Carleton College, where he received his bachelor’s degree in Chemistry with Distinction. He did research in carbohydrate chemistry with Professor Gary R. Gray at the University of Minnesota before entering graduate school at the Massachusetts Institute of Technology. There he returned to proteins in the laboratory of Professor Robert T. Sauer, using experimental and computational methods to probe and predict protein structure.
After completing his Ph.D. work, Bowie did postdoctoral work as a Life Sciences Research Foundation fellow with Professor David Eisenberg at UCLA, continuing work on structure prediction and structure determination by x-ray crystallography.
He joined the UCLA faculty in 1993 and is now a full professor. His current research focuses on fundamental and practical aspects of membrane protein folding and cell-free methods for the production of commodity chemicals and biofuels.
Bowie has served as President of the Protein Society, on NIH study sections, and on the editorial boards of the Journal of Molecular Biology, Protein Science, Biochemistry and Proteins. He has organized many meetings and co-founded a new Gordon Conference on Membrane Protein Folding. Bowie has been recognized as an NSF National Young Investigator, a Pew Scholar, a Leukemia and Lymphoma Society Scholar, a Dreyfus Foundation Mentor, a Fellow of the AAAS, the King’s College Higgs Lecturer, a McCoy Awardee, Biophysical Society Anatrace Awardee and a Biophysical Society Fellow. He is particularly proud to be given the UCLA Postdoctoral Mentoring award based on nominations by his students.
To learn more about Bowie’s research, visit his group’s website.
Penny Jennings, UCLA Department of Chemistry & Biochemsitry, penny@chem.ucla.edu.
