Dynamic transitions in coupled motor proteins.
The effect of interactions on dynamics of coupled motor proteins is investigated theoretically. A simple stochastic discrete model, which allows one to calculate explicitly the dynamic properties, is developed. It is shown that there are two dynamic regimes, depending on the interaction between the particles. For strong interactions the motor proteins move as one tight cluster, while for weak interactions there is no correlation in the motion of the proteins, and the particle separation increases steadily with time. The boundary between the two regimes is specified by a critical interaction that has a nonzero value only for the coupling of the asymmetric motor proteins, and it depends on the temperature and transition rates. At the critical interaction there is a change in slope for the mean velocities and a discontinuity in the dispersions of the motor proteins as a function of interactions.
Stukalin
Evgeny B
EB
Department of Chemistry, Rice University, Houston, Texas 77005, USA.
Kolomeisky
Anatoly B
AB
D001665:Binding Sites; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry*; D009038:Motion; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*
D020409:Molecular Motor Proteins; D011506:Proteins