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Single myosin molecule mechanics: piconewton forces and nanometre steps

Single myosin molecule mechanics: piconewton forces and nanometre steps 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Single myosin molecule mechanics: piconewton forces and nanometre steps

Nature , Volume 368 (6467) – Mar 10, 1994

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References (39)

Publisher
Springer Journals
Copyright
Copyright © 1994 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/368113a0
Publisher site
See Article on Publisher Site

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.

Journal

NatureSpringer Journals

Published: Mar 10, 1994

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