Abstract
The dynamics of motor protein molecules consisting of two subunits is investigated usingsimple discrete stochastic models. Exact steady-state analytical expressions are obtainedfor velocities and dispersions for any number of intermediate states and conformationsbetween the corresponding binding states of proteins. These models enable us to provide adetailed description and comparison of two different mechanisms of the motion of motorproteins along the linear tracks: the hand-over-hand mechanism, when the motion ofsubunits alternate; and the inchworm mechanism, when one subunit is always trailinganother one. It is shown that the proteins in the hand-over-hand mechanism movefaster and fluctuate more than the molecules in the inchworm mechanism. Theeffect of external forces on dynamic properties of motor proteins is also discussed.Finally, a quantitative method, based on experimental observations for singlemotor proteins, is proposed for distinguishing between two mechanisms of motion.
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