Maximum power operation of interacting molecular motors.
We study the mechanical and thermodynamic properties of different traffic models for kinesin which are relevant in biological and experimental contexts. We find that motor-motor interactions play a fundamental role by enhancing the thermodynamic efficiency at maximum power of the motors, as compared to the noninteracting system, in a wide range of biologically compatible scenarios. We furthermore consider the case where the motor-motor interaction directly affects the internal chemical cycle and investigate the effect on the system dynamics and thermodynamics.
Department of Physics and Astronomy, University of Aarhus, Ny Munkegade, Building 1520, DK-8000 Aarhus C, Denmark.
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Golubeva
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Imparato
D007700:Kinetics; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000378:metabolism*; D011485:Protein Binding; D013816:Thermodynamics
D020409:Molecular Motor Proteins