Contraction due to bimetallic, short-lived super-coiling in the helical, double stranded filaments of striated muscle.
The possibility of a super-coiling of the thin filament is studied. The bimetallic super-coiling might contribute to the power-stroke. The calculation of the axial shortening of the proposed super-coiling leads to a very surprising geometric fitting: the maximal axial shortening of the super-coiling, without any loop, of the thin filament segment (38.5 nm) is equal to the axial repeat of cross-bridges (14 nm). According to the present model, the sarcomere shortening is caused by the axial shortening of the super-coiled actin filament. The top-view of the super-coiled segment shows a dual half-circle form. There are experimental evidences for such a type of formation in electron micrographs. According to this model, the widely accepted sterically hidrance model on association of actin and myosin can be neglected. One of the main roles of calcium is to make the thin filament segment flexible enough for the association.
Hummel
Z
Z
Biophysics Department, University Medical School, Pécs, Hungary.
D008841:Actin Cytoskeleton / Q000502:physiology*; D000199:Actins / Q000502:physiology; D000818:Animals; D002118:Calcium / Q000502:physiology*; D008433:Mathematics; D008954:Models, Biological; D009119:Muscle Contraction / Q000502:physiology*; D009132:Muscles / Q000502:physiology* / Q000648:ultrastructure; D009218:Myosins / Q000502:physiology
D000199:Actins; D009218:Myosins; D002118:Calcium