Susan Marqusee PBD Faculty Scientist
Professor of Biochemistry and Molecular Biology,
Department of Molecular and Cell Biology, University of California, Berkeley
Contact
info:
Lawrence Berkeley National Laboratory
Physical Biosciences Division
One Cyclotron Road
Mailstop: Hildabrand Hall
Berkeley, California 94720
USA
Research Emphasis The long-term goal of our research is to understand the structural and
dynamic information encoded in the linear sequence of amino acids. Proteins
undergo an incredible transformation from one-dimensional sequence information
into complex three-dimensional shapes that carry out intricate cellular
functions. We still, however, don't have enough biophysical knowledge to
translate this sequence information into functional insights. For instance, many
proteins share the same native structure yet their cellular dynamics and
function, in other words their energy landscapes, are different. Our laboratory
uses a combination of biophysical, structural and computational techniques to
understand these features.
In addition to the native conformation, a protein sequence populates small fluctuations around the native state, partially unfolded forms and even the globally unfolded conformation. Such non-native states on the energy landscape are thought to play a determining function in many cellular processes such as translocation, protein synthesis, degradation, signaling and allostery. They are also prone to aggregation, a phenomena which has been implicated for many diseases (the so-called misfolding and amyloid diseases). Understanding the sequence determinants of the energy landscape is therefore fundamental to the biological process that proteins carry out as well as protein folding itself.
