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Issue 6, 2017
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A physical picture for mechanical dissociation of biological complexes: from forces to free energies

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Abstract

Single-molecule force spectroscopy is a powerful technique based on the application of controlled forces to macromolecules. In order to relate the measured response of the molecule to its equilibrium and dynamic properties, a suitable physical picture of the involved process is necessary. In this work, we introduce a plausible model for mechanical unbinding of some molecular complexes, based on a novel free energy profile. We combine two standard theoretical frameworks for analyzing force spectroscopy experiments on two protein:protein complexes, obtaining key magnitudes of the underlying free energy profile, which are only understood within the mentioned model. Additionally, we carry out detailed stochastic dynamics simulations to prove the validity of the analysis protocol and the reliability of the free energy profile. Remarkably, we can compare directly the obtained unbinding free energies with the previously known bulk binding free energies, bridging the gap between bulk and single molecule techniques.

Graphical abstract: A physical picture for mechanical dissociation of biological complexes: from forces to free energies

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Publication details

The article was received on 02 Nov 2016, accepted on 05 Jan 2017 and first published on 05 Jan 2017


Article type: Paper
DOI: 10.1039/C6CP07508H
Citation: Phys. Chem. Chem. Phys., 2017,19, 4567-4575
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    A physical picture for mechanical dissociation of biological complexes: from forces to free energies

    R. Tapia-Rojo, C. Marcuello, A. Lostao, C. Gómez-Moreno, J. J. Mazo and F. Falo, Phys. Chem. Chem. Phys., 2017, 19, 4567
    DOI: 10.1039/C6CP07508H

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