Physical review. A, General physics · 1985 · 65 citations · 32 references
Natural SciencesBiochemistryBiophysicsMolecular BiophysicsMolecular PhysicsStructural BiophysicsMuscle MechanicsMuscle PhysiologyMuscle TissueProtein DynamicsProtein StructureCharge Transfer InteractionsContractile ProteinsMuscle ContractionMyosin MechanicsNonlinear Initial Value ProblemsNonlinearitySkeletal Muscle ContractionSolitons
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 \ensuremath{\alpha}-helical polypeptides. In each helix there are three one-dimensional chains of peptide groups joined together by H bonds which stabilize the \ensuremath{\alpha}-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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Method for Solving the Korteweg-deVries Equation
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