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The dance of actin and myosin

A structural and spectroscopic perspective

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Abstract

Actin and myosin interact in a cyclic series of steps linked to the hydrolysis of ATP that are representative of an ancient and widespread molecular mechanism. Spectroscopic findings are related to the analysis of the actin and myosin structures and results from kinetics, fibers, single molecules, electron microscopy, genetics, and a variety of other biophysical and biochemical studies on actin and myosin to provide an overview of the steps in this molecular process. The synthesis of the key findings from these fields reveals a highly efficient engine that amplifies subtle changes in the active site into unsurpassed molecular displacements. Recent developments in resonance energy-transfer spectroscopy and X-ray crystallography are enabling a detailed elucidation of the stages of a large power stroke that concurs with evidences from diverse lines of structural and kinetic inquiry. A complete image of actin and myosin motility appears to include twists, tilts, steps, and dynamics from both partners that could be described as a molecular dance.

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  1. Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, P. O. Box 305220, 76203-5220, Denton, TX

    Douglas D. Root

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Correspondence to Douglas D. Root.

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Root, D.D. The dance of actin and myosin. Cell Biochem Biophys 37, 111–139 (2002). https://doi.org/10.1385/CBB:37:2:111

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