Touring the Protein Energy Landscape: The View Depends on How and When You Look

Tuesday, February 28, 2017 | 12:30 p.m. - 1:30 p.m. Add to Calendar

The Center for Theoretical Biological Physics PRESENTS Seminar Speaker Dr. Susan Marqusee Professor of Molecular and Cell Biology Division of Biophysics, Biochemistry and Structural Biology University of California, Berkeley “Touring the Protein Energy Landscape: The View Depends on How and When You Look”

Abstract: Understanding the structural and dynamic information encoded in the primary sequence of a protein is one of the most fundamental challenges in modern biology. The amino acid sequence of a protein encodes more than the native three-dimensional structure; it encodes the entire energy landscape – an ensemble of conformations whose energetics and dynamics are finely tuned for folding, binding and activity. Small variations in the sequence and environment modulate this landscape and can have effects that range from undetectable to pathological. I will present our recent results probing these sequence and environmental effects using a combination of single-molecule and ensemble-based studies. I will address a fundamental question in protein folding of whether proteins fold through one or multiple trajectories and its implications for protein folding in complex environments, and the suggestion that evolution can modulate both the rates of folding and the specific pathway.

Bio: Dr. Susan Marqusee is a Professor of Molecular and Cell Biology, Division of Biophysics, Biochemistry and Structural Biology, at the University of California, Berkeley. Since 2010, she has also served as the director of Berkeley’s Institute for Quantitative Biosciences (QB3). Marqusee received her A.B. in Physics and Chemistry from Cornell University in 1982, and her M.D. and Ph.D. degrees from Stanford University in 1990. After a post-doctoral fellowship at MIT, she joined the UC Berkeley faculty as Assistant Professor in 1992. Marqusee is one of the world’s top experimental scientists in the field of protein folding. She is known for many contributions, including the first de novo design of a short peptide that folds 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 some of the most detailed experimental views of a protein’s energy landscape. Marqusee is a member of the National Academy of Sciences, a fellow of the American Academy of Arts and Sciences, the American Association for the Advancement of Science, and the Biophysical Society In 2011 and 2012, the San Francisco Business Times recognized Marqusee as one of the top 150 “Most influential women in the Bay Area” and in 2012, she received the ASBMB William Rose Award for Science and Mentorship.


BioScience Research Collaborative, Room 1060 A/B

6500 Main St.


Lisa Bennett