Professor Charles L. Brooks, III
Department of Molecular Biology
The Scripps Research Institute
La Jolla, California

Monday, January 31, 2000
3:00 pm (CT)
3269 Beckman Institute

Abstract

The role of electrostatic interactions and dielectric response in modulating the thermal stability of proteins has been explored using simulation and continuum electrostatic theories. For proteins from a "thermophilic series", we demonstrate that two features contribute significantly to the enhanced stability of thermophilic proteins relative to their mesophilic counterparts. These features, the nature of electrostatic interactions of charged residues in the folded state and the dielectric response of the folded protein, provide a unifying picture of the extraordinary thermal stability characteristics of extremophiles which encompasses earlier ideas of enhanced protein dipoles, the role of salt bridges, etc. We will present arguments as to the origin of this observed enhanced stability as well as the role of these properties in cold denaturation of proteins. Finally, new "design" principles for engineering proteins with enhanced thermal stability will be examined.

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