Abstract:
Many biological processes are supported by special molecules, called motor proteins or molecular motors, that transport cellular cargoes along linear protein filaments and can reversibly associate to their tracks. Stimulated by these observations, we developed a theoretical model for collective dynamics of biological molecular motors that accounts for local association/dissociation events representing strong coupling of particles. In our approach, the particles interacting only via exclusion move along a lattice in the preferred direction, while the reversible associations are allowed at the specific site far away from the boundaries. Considering the association/dissociation site as a local defect, the inhomogeneous system is approximated as two coupled homogeneous sub-lattices. This allows us to obtain a full description of stationary dynamics in the system. It is found that the number and nature of steady-state phases strongly depend on the values of association and dissociation transition rates. Microscopic arguments to explain these observations as well as biological implications are also discussed. We then compare the dynamical properties of the proposed model with the earlier studied variant considering weakly coupled particles. Theoretical predictions agree well with extensive Monte Carlo computer simulations.