Actin as the generator of tension during muscle contraction.
We propose that the key structural feature in the conversion of chemical free energy into mechanical work by actomyosin is a myosin-induced change in the length of the actin filament. As reported earlier, there is evidence that helical actin filaments can untwist into ribbons having an increased intersubunit repeat. Regular patterns of actomyosin interactions arise when ribbons are aligned with myosin thick filaments, because the repeat distance of the myosin lattice (429 A) is an integral multiple of the subunit repeat in the ribbon (35.7 A). This commensurability property of the actomyosin lattice leads to a simple mechanism for controlling the sequence of events in chemical-mechanical transduction. A role for tropomyosin in transmitting the forces developed by actomyosin is proposed. In this paper, we describe how these transduction principles provide the basis for a theory of muscle contraction.
Schutt
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CE
Henry H. Hoyt Laboratory, Department of Chemistry, Princeton University, NJ 08544.
Lindberg
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D000199:Actins / Q000502:physiology* / Q000648:ultrastructure; D000205:Actomyosin / Q000502:physiology; D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D003196:Computer Graphics; D003285:Contractile Proteins; D003461:Crystallography; D006801:Humans; D008840:Microfilament Proteins / Q000648:ultrastructure; D008854:Microscopy, Electron; D008961:Models, Structural; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology* / Q000648:ultrastructure; D009218:Myosins / Q000502:physiology; D051304:Profilins; D014961:X-Ray Diffraction
D000199:Actins; D003285:Contractile Proteins; D008840:Microfilament Proteins; C495738:PFN1 protein, human; D051304:Profilins; D000205:Actomyosin; D009218:Myosins