Professor Evan Evans
School of Engineering
Duke University
Durham, North Carolina

Monday, November 11, 1996
3:00 pm (CT)
3269 Beckman Institute

Abstract

In biology, macromolecular linkages and complexes in biochemical pathways mainly involve weak-noncovalent interactions, which is reflected in a range of bond lifetimes from microseconds to many months. As such, biomolecular bonds form a diverse set of kinetic traps where bond strength is a transient property governed by far from equilibrium kinetics. Conversely, the kinetics of bond dissociation depend on applied force, which is likely to be an important factor in biochemical pathways. Some important questions are: What physics governs the force-driven dissociation of bonds and bond strength? How does molecular architecture affect bond strength? What can be learned from laboratory tests of bond strength and how should these tests be performed? To address these questions, we have extended Kramers' theory for kinetics in liquids to dissociation under force and compared the predictions of the theory to results obtained from smart Monte Carlo SMC (Brownian dynamics) simulations of bond rupture.

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