Dr. Ulrich H. E. Hansmann
Department of Physics
Michigan Technological University
Houghton, MI

Monday, January 26, 2004
3:00 pm (CT)
3269 Beckman Institute

Abstract

The successful deciphering of the human genom has highlighted newly an old challenge in protein science: for most of the resolved protein sequences we do not know the corresponding structures and functions. Neither do we understand in detail the mechanism by which a protein folds into its biologically active form. Computer experiments offer one way to evaluate the sequence-structure relationship and the folding process but are extremely difficult for detailed protein models. This is because the energy landscape of all-atom protein models is characterized by a multitude of local minima separated by high energy barriers. Only over the last few years have algorithms been developed that allow one to overcome this multiple- minima problem in protein simulations. Prominent examples of these new and sophisticated techniques are parallel tempering and generalized-ensemble sampling. The lecture will present applications of these methods to small proteins such as the 34-residue PTH(1-34) and the 36-residue villin headpiece subdomain HP-36.

Coffee will be served in R3151 Beckman Institute at 2:15pm.