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.

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