Physics Colloquium, October 28, 2003

Folding on rough energy landscapes

Martin Gruebele

University of Illinois at Urbana-Champaign
Departments of Chemistry, Physics and
Center for Biophysics and Computational Biology

During the last 10 years, quantitative concepts from statistical mechanics have given us a deeper microscopic understanding of the relationship between protein folding, function and structure. In addition, fast relaxation experiments and single molecule experiments have probed the full range of time scales from nanoseconds to milliseconds, and have begun to dissect "heterogeneous" behavior during folding. Because the weak couplings that provide the binding energy for proteins are not as directional as classical chemical bonds, a picture is emerging where folding is not along a single pathway, but explores multiple albeit reduced dimensions of the energy landscape in a "heterogeneous" process. Most of the barriers associated with motions on this landscape are very small, and it may be that large barriers arise mainly as a consequence of protein function frustrating the folding process. These ideas will be illustrated with experimental data, molecular dynamics simulations, and simple statistical mechanical models.

3.30 p.m., Smith Laboratory, Room 1005

Refreshments served in Smith 1094 at 3:00 p.m.