Recently, unusually high detachment rates of a myosin from actin were reported with a force spectroscopy technique. Here, we show that these high rates may be due to the coupling between bond breaking and state transition. Based on a kinetic model for single myosin, rates of bond breaking between myosin and actin at different nucleotide states are systematically extracted for the first time. Our results clearly indicate that myosins may adopt much higher transition rates than bond breaking rates at different nucleotide states at relatively low forces.
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