The distribution of the charged residues in myosin hinge region and its relationship to the distribution of charged residues in the rest of myosin rod.

Fourier transform analysis of the amino acid sequence of the hinge region from both rabbit skeletal myosin and nematode myosin indicates that the basic residues show strong periodicity of 25.7 residues whereas the periodicity of acidic residues is very weak. Other 100 residue segments of the rod sequence of nematode myosin show an alternation between regions in which the 28 residue repeat is predominantly basic and regions in which it is predominantly acidic. The strong basic and weak acidic near 28 residue repeat of the hinge region appears to form part of this pattern. This alternation suggests that the packing of myosin rods is more favourable when the neighbouring molecules are staggered by about 100 residues or odd multiples of 100 residues, which is consistent with the observed repeats (14.6 and 44.0 nm) of cross-bridges.