Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy: theory and applications

Biophysical Journal
V BarsegovD Thirumalai

Abstract

We present, to our knowledge, a new theory that takes internal dynamics of proteins into account to describe forced-unfolding and force-quench refolding in single molecule experiments. In the current experimental setup (using either atomic force microscopy or laser optical tweezers) the distribution of unfolding times, P(t), is measured by applying a constant stretching force f(S) from which the apparent f(S)-dependent unfolding rate is obtained. To describe the complexity of the underlying energy landscape requires additional probes that can incorporate the dynamics of tension propagation and relaxation of the polypeptide chain upon force quench. We introduce a theory of force correlation spectroscopy to map the parameters of the energy landscape of proteins. In force correlation spectroscopy, the joint distribution P(T, t) of folding and unfolding times is constructed by repeated application of cycles of stretching at constant f(S) separated by release periods T during which the force is quenched to f(Q) < f(S). During the release period, the protein can collapse to a manifold of compact states or refold. We show that P(T, t) at various f(S) and f(Q) values can be used to resolve the kinetics of unfolding as well as formation...Continue Reading

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Citations

Sep 24, 2008·Langmuir : the ACS Journal of Surfaces and Colloids·Laura Porter-PedenKumar Sinniah
Jun 23, 2009·Proceedings of the National Academy of Sciences of the United States of America·Sergi Garcia-ManyesJulio M Fernández
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Nov 15, 2011·Structure·Artem ZhmurovValeri Barsegov
Dec 13, 2017·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Olga KononovaValeri Barsegov
Nov 19, 2008·European Biophysics Journal : EBJ·Dmitry I ChernyClive R Bagshaw
Jan 9, 2009·Electrophoresis·Alexandr Jonás, Pavel Zemánek
Aug 8, 2020·The FEBS Journal·Sabita SharmaIonel Popa
Oct 19, 2017·Journal of the American Chemical Society·Kirill A MininValeri Barsegov

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