Abstract:
Motor proteins or biological molecular motors belong to a class of active enzymatic
molecules that are responsible for transport and force generation in living cells. They
typically operate in large teams and individual protein molecules interact with each
other while moving along linear cytoskeleton filaments. Moreover, during their transportation the motors can reversibly dissociate from their tracks. Motivated by these
observations, we propose a one dimensional totally asymmetric simple exclusion model
for interacting particles that are allowed to reversibly dissociate/associate from a particular site far away from the system boundaries. A theoretical analysis of the model is based
on cluster mean-field approximation that allows for a comprehensive description of the
stationary properties in the system. It is found that the topology and nature of stationary
phase diagrams for varying association/dissociation rates strongly depend on the sign
and strength of interactions. Extensive Monte Carlo simulations are implemented to test
our theoretical predictions.
