Movement and force produced by a single myosin head View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-11

AUTHORS

J. E. Molloy, J. E. Burns, J. Kendrick-Jones, R. T. Tregear, D. C. S. White

ABSTRACT

MUSCLE contraction is driven by the cyclical interaction of myosin with actin, coupled to the breakdown of ATP. Studies of the interaction of filamentous myosin1 and of a double-headed proteolytic fragment, heavy meromyosin (HMM)2,3, with actin have demonstrated discrete mechanical events, arising from stochastic interaction of single myosin molecules with actin. Here we show, using an optical-tweezers transducer2,4, that a single myosin subfragment-1 (S1), which is a single myosin head, can act as an independent generator of force and movement. Our analysis accounts for the broad distribution of displacement amplitudes observed, and indicates that the underlying movement (working stroke) produced by a single acto-Sl interaction is ~4 nm, considerably shorter than previous estimates1–3,5 but consistent with structural data6. We measure the average force generated by S1 or HMM to be at least 1.7 pN under isometric conditions. More... »

PAGES

209-212

Journal

TITLE

Nature

ISSUE

6553

VOLUME

378

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/378209a0

    DOI

    http://dx.doi.org/10.1038/378209a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1031755821

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7477328


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