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Muscle contraction

Myosin trapped but not tamed

Nature volume 390, pages 345–346 (1997)Cite this article

Muscle shortening involves interdigitation of actin- and myosin-containing filaments driven by the action of cross-bridges powered by ATP hydrolysis. The detailed mechanism remains in question, however, and current research has centred on definition of the structures of the cross-bridge (the head of the myosin molecule) and actin at atomic resolution, and the development of assays to follow mechanics and chemistry at the single-molecule level. At the annual European conference on muscleFootnote 1, new developments were announced in these areas, along with progress on other topics, including fresh ways of looking at muscle disease.

* XXVI European Muscle Congress , Schneverdingen, Germany, 21-25 September 1997. Abstracts to be published in J. Muscle Res. Cell Motility.

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Figure 1: Simultaneous measurement of ATPase and mechanical displacement by a single myosin head.

Notes

  1. * XXVI European Muscle Congress , Schneverdingen, Germany, 21-25 September 1997. Abstracts to be published in J. Muscle Res. Cell Motility.

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  1. the Department of Biochemistry, University of Leicester, Leicester, LE1 7RH, UK

    Clive R. Bagshaw

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  1. Clive R. Bagshaw
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Bagshaw, C. Myosin trapped but not tamed. Nature 390, 345–346 (1997). https://doi.org/10.1038/37002

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