  Kinesins are processive motor proteins that move along microtubules in a
stepwise manner, and their motion is powered by the hydrolysis of ATP. Recent
experiments have investigated the coupling between the individual steps of
single kinesin molecules and ATP hydrolysis, taking explicitly into account
forward steps, backward steps and detachments. A theoretical study of
mechanochemical coupling in kinesins, which extends the approach used
successfully to describe the dynamics of conventional motor proteins, is
presented. The possibility of irreversible detachments of kinesins from the
microtubules is also explicitly taken into account. Using the method of first-
passage times, experimental data on the mechanochemical coupling in kinesins
are fully described using the simplest two-state model. It is shown that the
dwell times for the kinesin to move one step forward or backward, or to
dissociate irreversibly are the same, although the probabilities of these
events are different. It is concluded that the current theoretical view, that
only the forward motion of the motor protein molecule is coupled to ATP
hydrolysis, is consistent with all available experimental observations for
kinesins.
