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- W2154535641 endingPage "728" @default.
- W2154535641 startingPage "687" @default.
- W2154535641 abstract "X-ray crystallography shows the myosin cross-bridge to exist in two conformations, the beginning and end of the power stroke. A long lever-arm undergoes a 60 degrees to 70 degrees rotation between the two states. This rotation is coupled with changes in the active site (OPEN to CLOSED) and phosphate release. Actin binding mediates the transition from CLOSED to OPEN. Kinetics shows that the binding of myosin to actin is a two-step process which affects ATP and ADP affinity. The structural basis of these effects is not explained by the presently known conformers of myosin. Therefore, other states of the myosin cross-bridge must exist. Moreover, cryoelectronmicroscopy has revealed other angles of the cross-bridge lever arm induced by ADP binding. These structural states are presently being characterized by site-directed mutagenesis coupled with kinetic analysis." @default.
- W2154535641 created "2016-06-24" @default.
- W2154535641 creator A5039484661 @default.
- W2154535641 creator A5052279487 @default.
- W2154535641 date "1999-06-01" @default.
- W2154535641 modified "2023-10-10" @default.
- W2154535641 title "Structural Mechanism of Muscle Contraction" @default.
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