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- W2016160482 abstract "Abstract It is now generally believed that the force necessary for muscle contraction results from a structural transition in the myosin crossbridge. Recent spectroscopic studies have indicated that myosin can exist in two distinct structural states. The equilibrium between the two states is poised in such a way that it can be forced in either direction with minor changes in experimental conditions. During ATP hydrolysis, myosin is forced to oscillate between the two states concomitantly with free energy dissipation. The chemical energy of ATP hydrolysis is transduced into a mechanical swithhing of the myosin structure between the two states. The myosin ATPase active site may be viewed as a time-dependent effector site responsible for the switching. Changes in the equilibrium between the two states have been shown to parallel changes in tension in muscle fibers. It is possible that the two myosin states may be directly correlated to the force-producing power stroke in muscle." @default.
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- W2016160482 date "1984-07-01" @default.
- W2016160482 modified "2023-09-26" @default.
- W2016160482 title "Energy transduction in myosin" @default.
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- W2016160482 doi "https://doi.org/10.1016/0968-0004(84)90303-7" @default.
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