Mechanics of the power stroke in myosin II.
Power stroke in skeletal muscles is a result of a conformational change in the globular portion of the molecular motor myosin II. In this paper we show that the fast tension recovery data reflecting the inner working of the power stroke mechanism can be quantitatively reproduced by a Langevin dynamics of a simple mechanical system with only two structural states. The proposed model is a generalization of the two state model of Huxley and Simmons. The main idea is to replace the rigid bistable device of Huxley and Simmons with an elastic bistable snap spring. In this setting the attached configuration of a cross bridge is represented not only by the discrete energy minima but also by a continuum of intermediate states where the fluctuation induced dynamics of the system takes place. We show that such soft-spin approach explains the load dependence of the power stroke amplitude and removes the well-known contradiction inside the conventional two state model regarding the time scale of the power stroke.
Marcucci
L
L
LMS, CNRS-UMR 7649, Ecole Polytechnique, 91128 Palaiseau, France.
Truskinovsky
L
L
D000255:Adenosine Triphosphate / Q000737:chemistry; D000465:Algorithms; D000818:Animals; D001696:Biomechanical Phenomena; D001703:Biophysics / Q000379:methods*; D004548:Elasticity; D006801:Humans; D007700:Kinetics; D008962:Models, Theoretical; D009119:Muscle Contraction; D024462:Myosin Type II / Q000737:chemistry*; D013269:Stochastic Processes; D013314:Stress, Mechanical
D000255:Adenosine Triphosphate; D024462:Myosin Type II