Susan Marqusee

University of California, Berkeley

Election Year: 2016
Primary Section: 29, Biophysics and Computational Biology
Secondary Section: 21, Biochemistry
Membership Type: Member


Susan Marqusee is a biophysical chemist whose work focuses on protein folding and dynamics. 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. Marqusee was born in New York and grew up in London England. She received her AB in Physics and Chemistry from Cornell University in 1982, and her PhD (Biochemistry) and MD degrees from Stanford University in 1990. After a post-doctoral fellowship at MIT, she joined the UC Berkeley faculty as Assistant Professor in 1992, advancing to Associate and Full Professor in 1998 and 2001 respectively. Since 2009, Marqusee has also served as the Berkeley director for the California Institute of Quantitative Biosciences (QB3). Marqusee has received the Beckman Young Investigator award, the Margaret Dayhoff Oakley award from the Biophysical Society, and the William Rose Award from the American Society of Biochemistry and Molecular Biology. She is a fellow of the American Academy of Arts and Sciences and the National Academy of Sciences.

Research Interests

Susan Marqusee’s laboratory is interested in deciphering the structural and dynamic information encoded in a protein’s amino-acid sequence with the ultimate goal of understanding and predicting how changes in the sequence or environment affect a protein’s energy landscape and function. She uses a combination of biophysical, structural, and computational techniques to both interrogate the energy landscape and develop new methodologies. The development of a single molecule optical tweezers approach to manipulate and observe protein conformational changes in real time provided the first glimpse of the unfolding and refolding trajectory of a single protein molecule. This approach has provided evidence for the on-pathway obligatory nature of an early folding intermediate and has identified new mechanical properties of proteins. Recent work has demonstrated the existence of parallel folding pathways in a simple two-state folding protein, clarifying an apparent discrepancy between experimental and theoretical studies and demonstrating that small changes in either the environment or sequence can alter the folding trajectory. The fundamental nature of Dr. Marqusee’s work has significant impact on many other areas of research, ranging from the physical chemistry of macromolecules to the design of therapeutics that prevent the aggregation of proteins which lead to common diseases such as Alzheimer’s.

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