Doctor Catherine Royer
CENTRE de BIOCHIMIE
UMR 5048 CNRS/Universite Montpellier I
Montpellier, France

Monday, October 22, 2001
3:00 pm (CT)
3269 Beckman Institute

Abstract

The thermodynamics of protein folding resembles that of the transfer of hydrophobic compounds to water in many respects. However, the response of protein structure to pressure is very different from that of hydrophobic model compounds. In fact, the pressure response is dictated by changes in packing and hydration upon protein conformational transitions and, thus, provides information about the specificity of protein structure and stability. High pressure fluorescence, SAXS, FTIR, NMR, and densitometry reveal the structural changes which occur upon the application of pressure to a number of protein systems and the kinetic behavior of these observables allows one to characterize the rate limiting step in protein folding.

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