Abstract
The mechanical processes generated by the molecular motors, myosin and actin, were measured using single molecule imaging, manipulation, and nanometry techniques. It was shown that the mechanical events of myosin are not tightly coupled with the ATP hydrolysis reaction and that myosin molecules move stochastically. These results indicate that the movement of myosin is driven by thermal motion rather than structural changes occurring in the myosin molecules. Thermal Brownian motion must be biased using the energy released from the hydrolysis of ATP. Thus, the molecular motors can harness thermal energy to perform mechanical work efficiently.
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