Thermodynamics and kinetics of a molecular motor ensemble.
If, contrary to conventional models of muscle, it is assumed that molecular forces equilibrate among rather than within molecular motors, an equation of state and an expression for energy output can be obtained for a near-equilibrium, coworking ensemble of molecular motors. These equations predict clear, testable relationships between motor structure, motor biochemistry, and ensemble motor function, and we discuss these relationships in the context of various experimental studies. In this model, net work by molecular motors is performed with the relaxation of a near-equilibrium intermediate step in a motor-catalyzed reaction. The free energy available for work is localized to this step, and the rate at which this free energy is transferred to work is accelerated by the free energy of a motor-catalyzed reaction. This thermodynamic model implicitly deals with a motile cell system as a dynamic network (not a rigid lattice) of molecular motors within which the mechanochemistry of one motor influences and is influenced by the mechanochemistry of other motors in the ensemble.
Baker
J E
JE
Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont 05405, USA. jbaker@salus.med.uvm.edu
Thomas
D D
DD
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D004735:Energy Transfer; D007700:Kinetics; D008024:Ligands; D046911:Macromolecular Substances; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics
D008024:Ligands; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins