Science / Technology - Colloquium
Monday, November 12, 2012
4:00 PM-5:00 PM
Nature has designed a large number of protein structures to perform specific functions. For physicists, proteins are superb laboratories for the exploration of the physics and chemistry of complex systems. Such studies are feasible because proteins does not exist in unique structures, but can assume a very large number of different conformations, called substates. The different substates can be characterized by the free-energy landscape. The transitions among the different substates are largely controlled from external fluctuations, the alpha fluctuations in the bulk solvent and the beta fluctuations in the hydration shell. This fact connects the protein physics to glasses and supercooled liquids, explains how function is controlled, and implies that the protein surface is as important as the interior.
Refreshments will be served in Olin Hall 118 at 3:30 P.M.
Suggested Audiences: College
Last Modified: November 6, 2012 at 11:32 AM