Kinetics of H-Bond Formation in Protein Folding

Professor Tobin R. Sosnick
Department of Biochemistry & Molecular Biology
Institute for Biophysical Dynamics
Chicago, Illinois

Monday, April 1, 2002
3:00 pm
3269 Beckman Institute

Abstract

The lecture will discuss when H-bonded structure forms during the folding of small proteins. According to our experimental and theoretical studies, early folding phases can reflect a generic response of the denatured ensemble to a change in solvent condition, rather than the formation of stable H-bonded structure. A comparison of foldable proteins and random sequences, however, indicates that the proteins develop additional 3-body correlations wherein a hydrophobic group stabilizes an H-bond, a difference that can be used to identify foldable sequences. In the later folding phase, a strong correlation is obtained using our kinetic isotope effect method between helical H-bond formation and surface burial in the folding transition state. This correlation is used to distinguish between various popular models for protein folding.

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