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Molecular mechanism of actin-myosin motor in muscle

Biochemistry (Moscow) volume 76, pages 1484–1506 (2011)Cite this article

Abstract

The interaction of actin and myosin powers striated and smooth muscles and some other types of cell motility. Due to its highly ordered structure, skeletal muscle is a very convenient object for studying the general mechanism of the actin-myosin molecular motor. The history of investigation of the actin-myosin motor is briefly described. Modern concepts and data obtained with different techniques including protein crystallography, electron microscopy, biochemistry, and protein engineering are reviewed. Particular attention is given to X-ray diffraction studies of intact muscles and single muscle fibers with permeabilized membrane as they give insight into structural changes that underlie force generation and work production by the motor. Time-resolved low-angle X-ray diffraction on contracting muscle fibers using modern synchrotron radiation sources is used to follow movement of myosin heads with unique time and spatial resolution under near physiological conditions.

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  1. Institute of Mechanics, Lomonosov Moscow State University, Michurinsky pr. 1, 119192, Moscow, Russia

    N. A. Koubassova & A. K. Tsaturyan

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  1. N. A. Koubassova
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  2. A. K. Tsaturyan
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Correspondence to N. A. Koubassova.

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Original Russian Text © N. A. Koubassova, A. K. Tsaturyan, 2011, published in Uspekhi Biologicheskoi Khimii, 2011, Vol. 51, pp. 233–282.

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Koubassova, N.A., Tsaturyan, A.K. Molecular mechanism of actin-myosin motor in muscle. Biochemistry Moscow 76, 1484–1506 (2011). https://doi.org/10.1134/S0006297911130086

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  • DOI: https://doi.org/10.1134/S0006297911130086

Key words

  • actin
  • myosin
  • muscle
  • ATPase
  • structure
  • X-ray diffraction