Professor Jose Onuchic
Department of Physics
University of California at San Diego
La Jolla, California

Monday, October 21, 2002
3:00 pm (CT)
3269 Beckman Institute

Abstract

Globally the energy landscape of a folding protein resembles a partially rough funnel. The local roughness of the funnel reflects transient trapping of the protein configurations in local free energy minima. The folding mechanisms for several fast folding proteins can be quantitatively described using an energy landscape theory to set up the correspondence with simulations of protein minimalist models. Using these simulations together with analytical theory, we can learn about good (minimallly frustrated) folding sequences and non-folding (frustrated) sequences. In adition to the need of minimizing energetic frustration, the topology of the native fold also plays a major role in the folding mechanism. Some folding motifs are easier to design than others suggesting the possibility that evolution not only selected sequences with sufficientlly small energetic frustration but also slected more easily designable native structures.

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