Protein folding in a force-clamp

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)

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Cited by in corpus (3)

• Mechanical unfolding and refolding pathways of ubiquitin
• New force replica exchange method and protein folding pathways probed by force-clamp technique
• The Interplay between Chemistry and Mechanics in the Transduction of a Mechanical Signal into a Biochemical Function