In recognition of her outstanding contributions to biophysics, the BPS Innovation Award has been renamed the Carolyn Cohen Award for Biophysical Innovation. The award, established in 2019, recognizes a BPS member who advances our fundamental understanding of biological systems through the development of novel theory, models, concepts, techniques, or applications.
The major objective of Carolyn Cohen’s work was to determine the precise molecular architecture of certain a-proteins that have dynamic as well as structural roles in the cell using X-ray crystallography together with molecular biology and biochemistry. Muscle proteins were a central focus that she used as a background for studying related systems. Her group visualized myosin in atomic detail in different stages of muscle contraction.
This motor is switched “on” and “off” by calcium ions which bind to regulatory proteins such as tropomyosin/troponin and—in certain cases—to myosin itself. Atomic structures of these switches showed how the motor activity is controlled.
She also worked on the protein folding problem, with a focus on the alpha-helical coiled-coil motif that occurs in a diverse range of proteins, including those in muscle (myosin rod, tropomyosin, paramyosin), membranes, and transcription factors (leucine zipper). The fact that this motif can be recognized easily and directly from the amino acid sequence of a protein gives it special significance. By making as many connections as possible among apparently diverse protein classes, her research yielded insights into the physical principles underlying protein folding.
Cohen was a member of the Biophysical Society from 1979 until she passed away in 2017. She received BPS’s 2000 Founders Award for outstanding achievement in Biophysics and was a Member of the National Academy of Sciences and a Fellow of the American Academy of Arts and Sciences.
The Carolyn Cohen Award for Biophysical Innovation will be presented next at the BPS 2022 Annual Meeting in San Francisco, California, on February 21.