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Muscle Contraction Mechanism Based on Actin Filament Rotation

  • Toshio Yanagida
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 592)

Abstract

Muscle contraction is caused by relative sliding movement between interdigitating actin and myosin filaments. It has been thought that myosin heads protruding from the myosin filament rotate between two orientations, while they repeat detachment from and attachment to actin filament coupled to the ATP hydrolysis cycle and the rotation of the head may cause the sliding. Recently atomic structure obtained from X-ray crystallography supports the rotation of the myosin head relative to the actin filament. A small conformational change in the ATP binding domain is transmitted to a neck domain that connects a motor domain (head) and tail domain, depending on the chemical state of nucleotide bound. Thus the neck domain acts as a lever-arm that can cause a displacement of 5–10 nm for the muscle myosin. This lever-arm swinging model has been a paradigm not only for the muscle myosin but also for unconventional myosins. Large stepsize of unconventional processive myosin V motor can be explained by its large lever arm within the frame of the lever-arm swinging model.

Keywords

Scanning Probe Myosin Head Actin Monomer Myosin Molecule Myosin Versus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer 2007

Authors and Affiliations

  • Toshio Yanagida
    • 1
  1. 1.Formation of Soft Nanomachines, Core Research for Evolution Science and Technology, Japan Science and Technology Agency, Department of Biophysical Engineering, Osaka University, Soft Biosystem Group, Laboratories for Nanobiology, Graduate School of Frontier BiosciencesOsaka UniversitySuita, OsakaJapan

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