Coulomb Interaction as the Source of Muscle Force
Abstract
Description
Myosin motor is the machine, which performs mechanical work in the course of adenosine triphosphate molecule hydrolysis and myosin head conformations accompanying this process. For displacement of individual fragments of large molecule relative to each other to arise and work to be performed, force must be born inside protein. What kind of interaction generates this force?
Models based on Huxley 1957 theory ascertain relations between chemical reactions rate constants and energies of crossbridge conformations. Nevertheless, understand in the framework of thermodynamics how myosin motor works in principle is impossible: it is smoothly heated device cyclically producing mechanical work (second law). Furthermore, in every working cycle myosin head captures and splits a single molecule. Hence, ordinary dynamic laws rather than stochastic laws govern this process.
The simple mechanism of chemomechanical transduction is proposed. The two products of adenosine triphosphate hydrolysis, adenosine diphosphate and inorganic phosphate, have charges of the same sense and Coulomb interaction of these charges produces the force pushing backdoor and rotating converter domain. The velocity of filaments sliding becomes the principal parameter in the model and new mechanism of indirect interaction between the cross-bridges radically different from one suggested by Huxley and Simmons in 1971 appears. The working stroke duration is inversely proportional to the velocity now. Therefore Hill equation appears and the parameter values obtained are in reasonable agreement with experiment.
23 pages, 2 figures
23 pages, 2 figures