The myosin cross-bridge alternates between two main conformations during the ATPase cycle, illustrating general principles of free energy transduction.
Muscle contraction occurs when the actin and myosin filaments in muscle are driven past each other by a cyclic interaction of adenosine triphosphate (ATP) and actin with cross-bridges that extend from myosin. Current biochemical studies suggest that, during each adenosine triphosphatase cycle, the myosin cross-bridge alternates between two main conformations, which differ markedly in their strength of binding to actin and in their overall structure. Binding of ATP to the cross-bridge induces the weak-binding conformation, whereas inorganic phosphate release returns the cross-bridge to the strong-binding conformation. This cross-bridge cycle is similar to the kinetic cycle that drives active transport and illustrates the general principles of free energy transduction by adenosine triphosphatase systems.
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Evan Eisenberg
National Institutes of Health
Terrell L. Hill
University of Maryland, Baltimore
Science
National Heart Lung and Blood Institute
National Institute of Diabetes and Digestive and Kidney Diseases
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Eisenberg et al. (Fri,) reported a review. The myosin cross-bridge alternates between two main conformations during the ATPase cycle, illustrating general principles of free energy transduction.
synapsesocial.com/papers/6a22507c00d082f62f972f16 — DOI: https://doi.org/10.1126/science.3156404