Peter Wolynes
Theoretical chemical physics; protein folding and function; glasses and stochastic cell biology
Contact Information
Office: UH 6202
Phone: (858) 822-4825
Fax: (858) 822-4560
Email: pwolynes@ucsd.edu
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Education and Appointments
1976 Ph.D., Harvard University
1971 A.B., Indiana University

Awards and Academic Honors
2009 2009-2010 Joseph O. Hirschfelder Prize in Theoretical Chemistry
2008 Biophysical Society, Founders Award
2007 Foreign Member, Royal Society (London)
2007 Member, German Academy of Sciences, Leopoldina
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: Interdisciplinary Specialties:
Physical/Analytical Chemistry Biophysics
Computational and Theoretical



Selected Publications
  • P.G. Wolynes, Energy Landscapes and Solved Protein Folding Problems, Phil. Trans. Roy. Soc. A, A363, 453-464 (2005).
  • M. Gruebele and P. G. Wolynes, Vibrational Energy Flow and Chemical Reactions, Acc. Chem. Res., 37, 261-267 (2004).
  • V. Lubchenko and P.G. Wolynes, Theory of Aging in Structural Glasses, J. Chem. Phys, 121, 2852-2865 (2004).
  • A.M. Walczak, M. Sasai and P.G. Wolynes, Self-consistent Proteomic Field Theory of Stochastic Gene Switches, Biophys. J., 88, 828-850 (2005).
  • J.D. Stevenson, J. Schmalian and P.G. Wolynes, The Shapes of Cooperatively Rearranging Regions in Glass Forming Liquids, Nature Physics, 21, 268-274 (2006).
  • C. Zong, G.A. Papoian, J. Ulander and P.G. Wolynes, "The Role of Topology, Nonadditivity and Water Mediated Interactions in Predicting the Structures of ±/² Proteins," J. Am. Chem. Soc., 128, 5168-5176 (2006).
  • T. Shen and P.G. Wolynes, Nonequilibrium Statistical Mechanical Models for Cytoskeletal Assembly: Towards Understanding Tensegrity in Cells," Phys. Rev. E, 72, 041927-11 (2005).
  • Ferreiro DU, Hegler JA, Komives EA, Wolynes PG, "Localizing frustration in native proteins and protein assemblies." Proc Natl Acad Sci U S A 50(19819-24): , 2007. [Go to PubMed]