| Abstract: | If the subfragment-2 (S2) portion of the myosin cross-bridge to actin does not lie parallel to the myofilament axes then when a muscle fiber contracts, there will be a radial component to the cross-bridge force. When the subfragment-1 (S1) portion of the cross-bridge attaches to actin with its long axis projecting through the filament axis, the magnitude of the radial force depends upon the azimuthal location of the actin site, but when the attachment of the S1 to actin is slewed, as in the reconstruction of Moore et al. (J. Mol. Biol., 1970, 50:279-294), then for a single cross-bridge the radial component of the cross-bridge force is not quite so sensitive to actin site location and is approximately 0.1 the axial component. In both cases, the ratio of the radial to axial force decreases with decreasing filament separation. If the radial-axial force ratio for each cross-bridge is approximately 0.1, then at full overlap in a frog skeletal muscle fiber the radial component of the cross-bridge force accompanying full activation will exert a compressive pressure of approximately 5 X 10(-3) atm. This would have little effect upon an intact muscle fiber where the volume constraints are likely osmotic, but it might produce a 1-2% change in filament spacing in a "skinned" muscle fiber from which the sarcolemma had been removed. These computations assume that the S2 link between the S1 head and the myosin filament does not support a bending moment of shear. If it does, then the radial component of the cross-bridge will be either greater or less, depending on the specific cross-bridge geometry. |
