Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy (FCS): Theory and applications

Details Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy (FCS): Theory and applications Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy (FCS): Theory and applications

2006-01-15

arxiv.org/abs/cond-mat/0601324v1

Physics

Condensed Matter

Soft Condensed Matter

23 pages, 9 figures; accepted to Biophysical Journal

Scientific paper

10.1529/biophysj.105.075937

In the current AFM experiments the distribution of unfolding times, P(t), is measured by applying a constant stretching force f_s from which the apparent 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 (FCS) to map the parameters of the energy landscape of proteins. In the FCS the joint distribution, P(T,t) of folding and unfolding times is constructed by repeated application of cycles of stretching at constant fs, separated by release periods T during which the force is quenched to f_q

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