  Biological transport is supported by collective dynamics of enzymatic
molecules that are called motor proteins or molecular motors. Experiments
suggest that motor proteins interact locally via short-range potentials. We
investigate the fundamental role of these interactions by analyzing a new class
of totally asymmetric exclusion processes where interactions are accounted for
in a thermodynamically consistent fashion. Theoretical analysis that combines
various mean-field cal- culations and computer simulations suggests that
dynamic properties of molecular motors strongly depend on interactions, and
correlations are stronger for interacting motor proteins. Surprisingly, it is
found that there is an optimal strength of interactions (weak repulsion) that
leads to a maxi- mal particle flux. It is also argued that molecular motors
transport is more sensitive to attractive interactions. Applications of these
results for kinesin motor proteins are discussed.
