West, D.K., Paci, E. and Olmsted, P.D. (2006) Internal protein dynamics shifts the distance to the mechanical transition state. Physical Review E : Statistical, Nonlinear and Soft Matter Physics, 74 (6). Art. No. 061912. ISSN 1550-2376
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2006 The American Physical Society. This is an author produced version of a paper subsequently published in Physical Review E. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) The University of Leeds > University of Leeds Research Centres and Institutes > Astbury Centre for Structural Molecular Biology (Leeds) |
Depositing User: | Repository Officer |
Date Deposited: | 08 Feb 2007 |
Last Modified: | 28 Oct 2016 08:16 |
Published Version: | http://link.aps.org/abstract/PRE/v74/e061912 |
Status: | Published |
Publisher: | American Physical Society |
Refereed: | Yes |
Identification Number: | 10.1103/PhysRevE.74.061912 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:1957 |