Abstract

Muscle contraction mechanism is discussed by reforming the model described in an article by Mitsui (Adv. Biophys. 1999, 36, 107–158). A simple thermodynamic relationship is presented, which indicates that there is an inconsistency in the power stroke model or the swinging lever model. To avoid this difficulty, a new model is proposed. It is assumed that a myosin head forms a polaron-like complex with about three actin molecules when it attaches to an actin filament and the complex translates along the actin filament producing force. Various experimental data on the muscle contraction are well explained based upon the model.

Highlights

  • Muscle contraction mechanism is discussed by reforming the model described in an article by Mitsui

  • The present authors and their colleagues [5, 6, 7], derived a simple thermodynamic relationship, showing that there is an inconsistency in the power stroke model

  • Difficulties in the power stroke model are discussed in Sect

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Summary

Introduction

The contraction of muscles takes place by mutual sliding of a thick (myosin) and a thin (actin) filaments. There is a recent review article on “Mechanics and models of the myosin motor” by Huxley [4]. The present authors and their colleagues [5, 6, 7], derived a simple thermodynamic relationship, showing that there is an inconsistency in the power stroke model. To avoid this difficulty, they proposed a new model from a completely different viewpoint. The model well explains various experimental data. Difficulties in the power stroke model are discussed in Sect. 2. Basic ideas of the new model are explained in Sect. A list of the parameter values used in calculation can be found in the Appendix

A thermodynamic relationship
Inconsistency in the power-stroke model
X-ray diffraction studies suggest constant r
Findings
Formation of molecular complex of myosin head and actin molecules
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