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.

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