The study provides structural evidence supporting a small hinge region in long myosin S2 fragments rather than an extensive helix-coil transition for contractile force.
Supports limited hinge in myosin S2; leaves open its role in contractile force pending functional validation.
The 270 MHz 1H NMR spectra of rabbit skeletal long and short S2 were indistinguishable at 20°C and 30°C and contained only a small proportion of sharp peaks associated with flexible regions. At 60°C both proteins were denatured and had essentially identical spectra. At 40°C and 50°C the long S2 spectrum contained a marginally greater proportion of sharp peaks, representing not more than 25 residues/chain. Our results are consistent with the presence of a small hinge in long S2 but do not support its containing an extensive region which provides contractile force by a helix—coil transition.
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Stewart et al. (1982) studied this question.
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