Doctor Gerhard Hummer
Laboratory of Chemical Physics, NIDDK
National Institutes of Health
Bethesda, Maryland

Monday, November 13, 2000
3:00 pm (CT)
3269 Beckman Institute

Abstract

Helix formation is an essential factor in protein folding. Extensive molecular dynamics simulations of short peptides in aqueous solution are used to study folding equilibria and kinetics of helix nucleation over a broad temperature range. Sequence effects on the folding kinetics can be understood from changes in the underlying energy landscape. A connection between the thermodynamics and kinetics of helix formation is established based on simple one-dimensional reaction coordinates, explaining the observed non- exponential relaxation kinetics. The rapid helix nucleation found here - in agreement with the analyses of laser temperature jump experiments - suggests that transient helices form early in protein folding events.

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