Linear electric traction as an alternative model of the actin/myosin motor.
Current models for the action of linear biological motors may be grouped in two main categories. The conventional "bind and bend" models rely for their power stroke upon a structural change in the myosin headgroup (S1 fragment) which follows the binding of myosin to the F-actin filament. The more recent ratchet models demonstrate that directional motion of a particle along an asymmetrical ratchet is possible with a symmetrical but time-correlated stochastic drive. In this paper a new type of model is introduced which is deterministic like the "bind and bend" model but it requires no molecular structural changes to power the stroke. Like the ratchet models the motor is driven along the linear stator by tangential forces at the interface but the forces are electrostatic and controlled by the hydrolysis of ATP to ADP.
Edmonds
D T
DT
Clarendon Laboratory, Oxford, U.K.
D000199:Actins / Q000502:physiology*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D004594:Electrophysiology; D006868:Hydrolysis; D008954:Models, Biological; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000502:physiology*
D000199:Actins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D009218:Myosins