Professor Dave Thirumalai
Institute for Physical Science and Technology
University of Maryland
College Park, Maryland

Monday, December 4, 2000
3:00 pm (CT)
144 Loomis

Abstract

The majority of proteins in cells fold spontaneously to the native conformation. However, a small number of proteins requires the assistance of molecular chaperones to reach the folded state. The molecular chaperones belong to the family of heat shock proteins. The most widely studied in this class of molecular machines is the chaperonin (GroEL) from E. coli. I will discuss the plausible mechanisms by which GroEL-assisted folding occurs. The predictions, based on computations using simple models, will be compared with recent experiments. The theoretical studies point to the need for single molecule studies in elucidating the key steps involved in the chaperonin- mediated folding of proteins.

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