Abstract
Myosin V, a two-headed motor protein, moves along actin filaments toward the positive end. Similar to other molecular motors, myosin V hydrolyzes Adenosine tri-phosphate (ATP) and releases its product to produce movement. This study proposes a multiple-paths model that considers the hydrolysis processes of catalytic sites at the two heads of myosin V as independent. The proposed model describes the myosin V transition process by seven states, with one load-dependent transition rate among these states. This model demonstrates how myosin V steps forward at different chemical reaction paths. This study also uses the enzyme kinetics to calculate the mean velocity. Stochastic processes are used to analyze the randomness as well. Analytical results reveal that the theoretical mean velocities, mean movement lengths, and randomness with various ATP concentrations under external load agree with the experimental data.
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