Skip to main content
Article thumbnail
Location of Repository

Internal protein dynamics shifts the distance to the mechanical transition state

By D.K. West, E. Paci and P.D. Olmsted

Abstract

Mechanical unfolding of polyproteins by force spectroscopy provides valuable insight into their free energy landscapes. Most experiments of the unfolding process have been fit to two-state and/or one dimensional models, with the details of the protein and its dynamics often subsumed into a zero-force unfolding rate and a distance x(u)(1D) to the transition state. We consider the entire phase space of a model protein under a constant force, and show that x(u)(1D) contains a sizeable contribution from exploring the full multidimensional energy landscape. This effect is greater for proteins with many degrees of freedom that are affected by force; and surprisingly, we predict that externally attached flexible linkers also contribute to the measured unfolding characteristics

Publisher: American Physical Society
Year: 2006
OAI identifier: oai:eprints.whiterose.ac.uk:1957

Suggested articles


To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.