Abstract

The present understanding of the relationship between the structure of the myosin ATPase and its role in force production for muscle contraction is reviewed. Emphasis is placed on structural transitions in myosin that occur during ATP hydrolysis which may be correlated with force production. Although detailed structural information is presently lacking, numerous spectroscopic and kinetic experiments have indicated that myosin exists in two structural states for each chemical intermediate in the hydrolysis of ATP. Models are discussed which view a transition between these two states as the energy transduction "event" (i.e., force production).

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