Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle

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Abstract
The amino acid sequence of the rod portion of nematode myosin, deduced from the sequence of the unc-54 H chain gene of Caenorhabditis elegans, is highly repetitive and has the characteristics of an .alpha.-helical coiled coil. The molecular surface contains alternate clusters of positive and negative charge. Interactions between charge clusters on adjacent molecules could account for the observed spacings of the myosin cross-bridges in muscle. The N-terminal third of the rod is evidently only loosely associated with the thick filament backbone. Bending of the rod near the end of this region could allow the N-terminal section to act as a hinged arm during muscle contraction.