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  On artifacts in single-molecule force spectroscopy

Cossio, P., Hummer, G., & Szabo, A. (2015). On artifacts in single-molecule force spectroscopy. Proceedings of the National Academy of Sciences of the United States of America, 112(46), 14248-14253. doi: 10.1073/pnas.1519633112.

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 Creators:
Cossio, Pilar1, Author           
Hummer, Gerhard1, Author           
Szabo, Attila2, Author
Affiliations:
1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
2Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA, ou_persistent22              

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Free keywords: anisotropic diffusion; free energy surface; pulling device; unfolding rate
 Abstract: In typical force spectroscopy experiments, a small biomolecule is attached to a soft polymer linker that is pulled with a relatively large bead or cantilever. At constant force, the total extension stochastically changes between two (or more) values, indicating that the biomolecule undergoes transitions between two (or several) conformational states. In this paper, we consider the influence of the dynamics of the linker and mesoscopic pulling device on the force-dependent rate of the conformational transition extracted from the time dependence of the total extension, and the distribution of rupture forces in force-clamp and force-ramp experiments, respectively. For these different experiments, we derive analytic expressions for the observables that account for the mechanical response and dynamics of the pulling device and linker. Possible artifacts arise when the characteristic times of the pulling device and linker become comparable to, or slower than, the lifetimes of the metastable conformational states, and when the highly anharmonic regime of stretched linkers is probed at high forces. We also revisit the problem of relating force-clamp and force-ramp experiments, and identify a linker and loading rate-dependent correction to the rates extracted from the latter. The theory provides a framework for both the design and the quantitative analysis of force spectroscopy experiments by highlighting, and correcting for, factors that complicate their interpretation.

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Language(s): eng - English
 Dates: 2015-09-152015-11-042015-11-17
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1519633112
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 112 (46) Sequence Number: - Start / End Page: 14248 - 14253 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230