Abstract
The force of muscle contraction is thought to be generated by a change in the effective angle of a myosin cross-bridge while it is attached to an actin filament. Thus studies of the relationship between this conformation and force provide insight into the mechanism of contraction. Recently it has been shown1 that paramagnetic probes can be attached selectively and rigidly to a reactive sulphydryl on the myosin cross-bridge and that their angular distribution can be measured with great accuracy. In rigor skeletal fibres the probes are highly ordered relative to the fibre axis. Here I show that forces of up to 0.2 N mm−2 cause no change in the angular distribution of the probes. Thus there is a domain of the cross-bridge whose conformation is not influenced by stress, and this result places restrictions on the location of elastic and force-generating elements within the cross-bridge.
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Cooke, R. Stress does not alter the conformation of a domain of the myosin cross-bridge in rigor muscle fibres. Nature 294, 570–571 (1981). https://doi.org/10.1038/294570a0
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DOI: https://doi.org/10.1038/294570a0
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