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1 H NMR study of long and short myosin S2 fragments
Author(s) -
Stewart Murray,
Roberts Gordon C.K.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80937-x
Subject(s) - chemistry , myosin , nmr spectra database , crystallography , spectral line , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , stereochemistry , physics , biochemistry , astronomy
The 270 MHz 1 H 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.