Protein folding in a force-clamp
arXiv:q-bio/0603018 · doi:10.1063/1.2192768
Abstract
Kinetics of folding of a protein held in a force-clamp are compared to an unconstrained folding. The comparison is made within a simple topology-based dynamical model of ubiquitin. We demonstrate that the experimentally observed variations in the end-to-end distance reflect microscopic events during folding. However, the folding scenarios in and out of the force-clamp are distinct.
9 pages, 4 figures, Journal of Chemical Physics (in press)