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  • Title: Internal protein dynamics shifts the distance to the mechanical transition state.
    Author: West DK, Paci E, Olmsted PD.
    Journal: Phys Rev E Stat Nonlin Soft Matter Phys; 2006 Dec; 74(6 Pt 1):061912. PubMed ID: 17280101.
    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.
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