  Motor proteins are active enzyme molecules that play a crucial role in many
biological processes. They transform the chemical energy into the mechanical
work and move unidirectionally along rigid cytoskeleton filaments.
Single-molecule experiments suggest that motor proteins, consisting of two
motor domains, move in a hand-over-hand mechanism when each subunit changes
between trailing and leading positions in alternating steps, and these subunits
do not interact with each other. However, recent experiments on heterodimeric
kinesins suggest that the motion of motor domains is not independent, but
rather strongly coupled and coordinated, although the mechanism of these
interactions are not known. We propose a simple discrete stochastic model to
describe the dynamics of homodimeric and heterodimeric two-headed motor
proteins. It is argued that interactions between motor domains modify free
energy landscapes of each motor subunit, and motor proteins still move via the
hand-over-hand mechanism but with different transitions rates. Our calculations
of biophysical properties agree with experimental observations. Several ways to
test the theoretical model are proposed.
