Reconstructing folding energy landscapes by single-molecule force spectroscopy

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Journal titleAnnual Review of Biophysics
Pages1939; # of pages: 21
Subjectarticle; conformation; diffusion coefficient; DNA hairpin; energy; equilibrium constant; feedback system; force; measurement; optical tweezers; priority journal; protein folding; protein function; protein structure; signal transduction; single molecule force spectroscopy; spectroscopy; structure activity relation
AbstractFolding may be described conceptually in terms of trajectories over a landscape of free energies corresponding to different molecular configurations. In practice, energy landscapes can be difficult to measure. Single-molecule force spectroscopy (SMFS), whereby structural changes are monitored in molecules subjected to controlled forces, has emerged as a powerful tool for probing energy landscapes. We summarize methods for reconstructing landscapes from force spectroscopy measurements under both equilibrium and nonequilibrium conditions. Other complementary, but technically less demanding, methods provide a model-dependent characterization of key features of the landscape. Once reconstructed, energy landscapes can be used to study critical folding parameters, such as the characteristic transition times required for structural changes and the effective diffusion coefficient setting the timescale for motions over the landscape. We also discuss issues that complicate measurement and interpretation, including the possibility of multiple states or pathways and the effects of projecting multiple dimensions onto a single coordinate. Copyright © 2014 by Annual Reviews. All rights reserved.
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AffiliationNational Research Council Canada (NRC-CNRC); National Institute for Nanotechnology (NINT-INNT)
Peer reviewedYes
NPARC number21272274
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Record identifierff9ceb6b-c6d3-4201-b3cd-a1466060de16
Record created2014-07-23
Record modified2016-05-09
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