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 xu 1D to the transition state. We consider the entire phase space of a model protein under a constant force, and show that xu 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. © 2006 The American Physical Society.

Internal protein dynamics shifts the distance to the mechanical transition state

Paci E.;
2006

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 xu 1D to the transition state. We consider the entire phase space of a model protein under a constant force, and show that xu 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. © 2006 The American Physical Society.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/886271
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