NANO-KINETICS
Ken Dill
School of Pharmacy
University of California, San Francisco
Wednesday, November 3, 2010
11:00 am – 12 pm
Fung Auditorium
Abstract:
We are interested in the dynamical laws — Fick’s law of particle diffusion, Fourier’s law of heat flow, and mass-action models of chemical kinetics, for example — in the limit of small system size. For example, biological cells often have small numbers of particles. How do the fluctuations matter? We have explored a theoretical approach to dynamics called Maximum Caliber, akin to Maximum Entropy for equilibria that treats full dynamical distribution functions of rates. In companion studies, we have developed experimental tests, including colloidal particle diffusion under a microscope, and single-particle A -->B reactions. Maximum Caliber appears to provide a general first-principles approach to treating single-molecule and few particle stochastic dynamical processes.
Biosketch:
Ken A Dill is a Distinguished Professor of Biophysics and Associate Dean of Research, School of Pharmacy, at the University of California, San Francisco. Dill received S.B. and S.M. degrees from MIT in Mechanical Engineering, a PhD in Biology with BH Zimm at the University of California, San Diego, and did postdoctoral research with PJ Flory in Chemistry at Stanford University. He received the first Hans Neurath Award in 1998, from the Protein Society, for his research on the structures of proteins. He co-founded a coalition of basic research societies that has advocated for bridging the physical and life sciences, was president of the Biophysical Society, and was elected to the National Academy of Sciences in 2008. With Sarina Bromberg, he co-authored Molecular Driving Forces, a textbook in physical chemistry and statistical mechanics.
Dill studies the physical principles of protein folding, the physics of water, and nonequilibrium statistical thermodynamics in small systems. He is known for his work elucidating: (1) that protein folding occurs on funnel-shaped energy landscapes, (2) the role of hydrophobic interactions in determining the structures of proteins, and (3) for developing, with Dr. Ron Zuckermann, a new class of protein-like polymer materials, called peptoids, that can fold and function much like biological molecules.