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 1550-2376Full text available as:
Available under licence : See the attached licence file.
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.
|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.|
|Institution:||The University of Leeds|
|Academic Units:||The University of Leeds > Faculty of Maths and 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:||09 Jun 2014 19:36|
|Publisher:||American Physical Society|