Myosin molecules are motor enzymes that convert chemical energy (e.g., from ATP hydrolysis) into mechanical work. Using spectroscopic, optical, and single molecule mechanics techniques, we have shown that myosin motors generate force with a large and discrete rotation of a lever-like domain upon binding actin tracks. Interestingly, in addition to generating force, myosin motor biochemical transitions are affected by force. Indeed, our studies imply that the mechanical behaviors of collective myosin systems, like myosin V and muscle, emerge from the interplay between myosin’s force-generating and force-sensing biochemistry. We have modeled these complex communication pathways in both small and large myosin ensembles.
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