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Single myosin molecule mechanics: piconewton forces and nanometre steps

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Abstract

A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament. Discrete stepwise movements averaging 11 nm were seen under conditions of low load, and single force transients averaging 3–4 pN were measured under isometric conditions. The magnitudes of the single forces and displacements are consistent with predictions of the conventional swinging-crossbridge model of muscle contraction.

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Author notes

  1. James A. Spudich: To whom correspondence should be addressed

Authors and Affiliations

  1. Departments of Biochemistry and Developmental Biology, Beckman Center, Stanford University School of Medicine, Stanford, California, 94305, USA

    Jeffrey T. Finer & James A. Spudich

  2. MRC Muscle and Cell Motility Unit, Randall Institute, King's College London, 26–29 Drury Lane, London, WC2B 5RL, UK

    Robert M. Simmons

Authors
  1. Jeffrey T. Finer
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  2. Robert M. Simmons
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  3. James A. Spudich
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Finer, J., Simmons, R. & Spudich, J. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature 368, 113–119 (1994). https://doi.org/10.1038/368113a0

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  • DOI: https://doi.org/10.1038/368113a0

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