Professor Sebastian Doniach
Applied Physics and Physics
Stanford University
Unknown Location

Sunday, October 17, 1999
3:00 pm (CT)
3269 Beckman Institute

Abstract

Folding of proteins from the denatured to native state is a very complex dynamical process. In recent years it has become clear that one cannot define a single pathway in the ordinary sense of chemical reactions, but that a proper description of folding must involve a multitude of pathways defining various transition state ensembles which help to nucleate the folding process. Time-resolved small-angle x-ray scattering data will be presented which demonstrate the diversity of folding processes for different small proteins. A new approach to computer simulation of the folding process at atomic resolution will be presented in which the statistics of different folding pathways is sampled by reaction path annealing.

Tea and coffee will be served in R3151 Beckman Institute at 2:15pm.