How muscle may contract.
A new molecular model is proposed for muscle contraction, that involves the electrical charging of the long (C-terminal) alpha-helical part of the head of the myosin molecule (S1) while the head is attached to actin; as it charges the alpha-helical part moves in the radial electric field between the filaments. The alpha-helical part snaps back when the myosin molecule is discharged electrically, at the moment that ATP binds to the active enzymatic site. This snap-back model explains several puzzling phenomena in contractility, as well as providing a physical explanation for the origin of an impulsive force that drives muscle contraction.
Open University Oxford Research Unit, UK.
G F
GF
Elliott
C R
CR
Worthington
D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004574:Electromagnetic Fields; D008954:Models, Biological; D008958:Models, Molecular; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000502:physiology*
D000199:Actins; D000255:Adenosine Triphosphate; D009218:Myosins