Anomalously increased lifetimes of biological complexes at zero force due to the protein-water interface

The Journal of Physical Chemistry. B
Yuriy V PereverzevEvgeni V Sokurenko

Abstract

A number of biological bonds show dramatically increased lifetimes at zero-force conditions, compared to lifetimes when even a small tensile force is applied to the ligand. The discrepancy is so great that it cannot be explained by the traditional receptor-ligand binding models. This generic phenomenon is rationalized here by considering the interaction of water with the receptor-ligand complex. It is argued that the water-protein interaction creates an energy barrier that prevents the ligand unbinding in the absence of the force. The properties of the interaction are such that even application of a relatively low force results in a dramatic drop of the bond lifetime due to the alteration of the water-receptor and water-ligand interaction network. The phenomenon is described by the presence of a second shallow interaction energy minimum for the bound ligand followed by a wide receptor-ligand dissociation barrier. The general analysis is applied quantitatively to the actin-myosin system, which demonstrates the gigantic drop of the bond lifetime at small forces and catch behavior (an increase in the lifetime) at moderate forces. The base hypothesis proposed to explain the small-force abnormal drop in the bond lifetime suggests th...Continue Reading

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Citations

Aug 26, 2010·The Journal of Physical Chemistry. B·Yuriy V PereverzevEvgeni V Sokurenko
Apr 12, 2015·Biophysical Journal·Alexander HarderDario Anselmetti
Oct 19, 2011·Biophysical Journal·Yuriy V PereverzevEvgeni V Sokurenko
Apr 1, 2009·Accounts of Chemical Research·Oleg V Prezhdo, Yuriy V Pereverzev

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