title: Mesoscopic non-equilibrium thermodynamic analysis of molecular motors.
abstract: We show that the kinetics of a molecular motor fueled by ATP and operating between a deactivated and an activated state can be derived from the principles of non-equilibrium thermodynamics applied to the mesoscopic domain. The activation by ATP, the possible slip of the motor, as well as the forward stepping carrying a load are viewed as slow diffusion along a reaction coordinate. Local equilibrium is assumed in the reaction coordinate spaces, making it possible to derive the non-equilibrium thermodynamic description. Using this scheme, we find expressions for the velocity of the motor, in terms of the driving force along the spacial coordinate, and for the chemical reaction that brings about activation, in terms of the chemical potentials of the reactants and products which maintain the cycle. The second law efficiency is defined, and the velocity corresponding to maximum power is obtained for myosin movement on actin. Experimental results fitting with the description are reviewed, giving a maximum efficiency of 0.45 at a myosin headgroup velocity of 5 × 10(-7) m s(-1). The formalism allows the introduction and test of meso-level models, which may be needed to explain experiments.
authors.affiliation: Department of Chemistry, Norwegian University of Science and Technology, 4791 Trondheim, Norway. signe.kjelstrup@ntnu.no.
authors.forename: S
authors.initials: S
authors.lastname: Kjelstrup
authors.forename: J M
authors.initials: JM
authors.lastname: Rubi
authors.forename: I
authors.initials: I
authors.lastname: Pagonabarraga
authors.forename: D
authors.initials: D
authors.lastname: Bedeaux
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D019277:Entropy; D007700:Kinetics; D008962:Models, Theoretical; D009218:Myosins / Q000378:metabolism*
chemical_list: D000255:Adenosine Triphosphate; D009218:Myosins