Thus, we discuss the mechanism and the evolution of the interaction in this molecular sliding system. The significance of the coincidence suggests a unit of interaction. The in vivo interaction specified here predicts the step size per cross bridge that correlates with the size of the actin molecule. From our model, we further predicted the twisted degrees of actin filament at contraction, the sliding distance per ATP hydrolysis, and the unitary velocity produced by a single cross bridge. Our predictions are compared with the experimental results reported up to now.
Muscle is considered to have evolutionary relationship with the cell transfer system.
We would like to discuss the possibility of sharing ATP hydrolysis energy with some myosin heads in the striated muscle and other excellent character that we can not expect from an independent interaction of a single myosin-like molecule and actin filament.