Peter Wolynes
Theoretical chemical physics; protein folding and function; glasses and stochastic cell biology

Contact Information
Adjunct Professor of Chemistry and Biochemistry

Office: Urey Hall
Phone:
Email: pwolynes@ucsd.edu
Web: chemistry.rice.edu/FacultyDetail.aspx?p=ACC7DC090095C11C
Education
1976 Ph.D., Harvard University
1971 A.B., Indiana University
Awards and Academic Honors
2011
University of Cambridge, Linnett Professorship at Sidney Sussex College,
2010
Honorary Doctorate, University of Stockholm
2010
Einstein Chair Professorship, Chinese Academy of Sciences
2009
2009-2010 Joseph O. Hirschfelder Prize in Theoretical Chemistry
2008
Biophysical Society, Founders Award
2007
Member, German Academy of Sciences, Leopoldina
2007
Foreign Member, Royal Society (London)
2006
Member, American Philosophical Society
2004
American Physical Society, Biological Physics Prize
2003
Fellow, Biophysical Society
2001-
Francis Crick Chair in the Physical Sciences, U.C. San Diego
2000
American Chemical Society Peter Debye Award in Physical Chemistry
1994
Fogarty Scholar in Residence N. I. H.
1991
Member, National Academy of Sciences
1991
Fellow American Academy of Arts and Sciences
1988
Fresenius Award of Phi Lambda Upsilon
1986-1987
John Guggenheim Fellow
1986
American Chemical Society Award in Pure Chemistry
1981-1983
Alfred P. Sloan Fellow,
Research Interests
The research in my group is broadly concerned with many-body phenomena in biology, chemistry and physics. A major theme is understanding systems where a large diversity of long lived states is involved, necessitating the use of a statistical characterization of an energy or attractor landscape. The most notable examples are glasses, liquids, biomolecules and biomolecular regulatory networks. In the area of protein folding we are interested both in describing folding kinetics in the laboratory and the development of bioinformatically based schemes for predicting structure from sequence using computer simulation. A key concept is that the energy landscape of a foldable protein looks like a rugged funnel. This idea guides the development of both simple folding kinetics models and structure prediction algorithms. Our prediction algorithms have already shown success in folding smaller proteins whose structure was previously unknown. Similar issues of attractor landscapes also arise in higher order biological processes, such as gene recognition and genetic network regulation, which we are beginning to study. The energy landscapes of supercooled liquids and glasses also present interesting problems. We have shown how a new approach based on "random first order transitions" explains many quantitative relations found empirically both in liquids and under cryogenic conditions where quantum effects play a role. The same ideas show promise in the study of systems as different as high temperature superconductors, polymer assemblies, and microemulsions. They may also be useful for describing the three dimensional structure and dynamics of the interior of living cells.

Primary Research Area
Physical/Analytical Chemistry
Interdisciplinary interests
Biophysics
Computational and Theoretical

Selected Publications