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Theory of rapid force spectroscopy

Author

Listed:
  • Jakob T. Bullerjahn

    (Universität Leipzig, Institut für theoretische Physik)

  • Sebastian Sturm

    (Universität Leipzig, Institut für theoretische Physik)

  • Klaus Kroy

    (Universität Leipzig, Institut für theoretische Physik)

Abstract

In dynamic force spectroscopy, single (bio-)molecular bonds are actively broken to assess their range and strength. At low loading rates, the experimentally measured statistical distributions of rupture forces can be analysed using Kramers’ theory of spontaneous unbinding. The essentially deterministic unbinding events induced by the extreme forces employed to speed up full-scale molecular simulations have been interpreted in mechanical terms, instead. Here we start from a rigorous probabilistic model of bond dynamics to develop a unified systematic theory that provides exact closed-form expressions for the rupture force distributions and mean unbinding forces, for slow and fast loading protocols. Comparing them with Brownian dynamics simulations, we find them to work well also at intermediate pulling forces. This renders them an ideal companion to Bayesian methods of data analysis, yielding an accurate tool for analysing and comparing force spectroscopy data from a wide range of experiments and simulations.

Suggested Citation

  • Jakob T. Bullerjahn & Sebastian Sturm & Klaus Kroy, 2014. "Theory of rapid force spectroscopy," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5463
    DOI: 10.1038/ncomms5463
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    Cited by:

    1. A. Barbier-Chebbah & O. Bénichou & R. Voituriez & T. Guérin, 2024. "Long-term memory induced correction to Arrhenius law," Nature Communications, Nature, vol. 15(1), pages 1-7, December.
    2. Rong Zhu & Daniel Canena & Mateusz Sikora & Miriam Klausberger & Hannah Seferovic & Ahmad Reza Mehdipour & Lisa Hain & Elisabeth Laurent & Vanessa Monteil & Gerald Wirnsberger & Ralph Wieneke & Robert, 2022. "Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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