Solitary excitations in muscle proteins

S. Yomosa
Phys. Rev. A 32, 1752 – Published 1 September 1985
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Abstract

In order to elucidate the molecular mechanism of muscle contraction, we propose a theory of nonlinear lattice solitons in muscle proteins. In a superstructure of myosin molecules, there are two α-helical polypeptides. In each helix there are three one-dimensional chains of peptide groups joined together by H bonds which stabilize the α-helical structure. Since the H-bonding interaction between peptide groups has a remarkable nonlinearity due to its charge-transfer interaction, we can regard a H-bonded chain of peptide groups as a one-dimensional nonlinear lattice. By using the earlier results of theoretical studies for nonlinear lattice solitons and for the initial-value problems, we can describe the molecular mechanism in the processes of the contraction of muscle.

  • Received 12 February 1985

DOI:https://doi.org/10.1103/PhysRevA.32.1752

©1985 American Physical Society

Authors & Affiliations

S. Yomosa

  • Sugiyama Jogakuen University, Nagoya 464, Japan

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Vol. 32, Iss. 3 — September 1985

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