N.M.R. studies of myelin basic protein. VII. Concentration and temperature dependence of amide resonances of the guinea pig encephalitogen in dimethyl sulfoxide

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Abstract
The encephalitogenic peptide comprising residues 114-122 in human myelin basic protein, Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Arg, has been studied by proton magnetic resonance at 400 MHz in dimethyl sulfoxide solutions. Temperature coefficients of the chemical shifts of the amide resonances of Glu6, Gly7 and Arg9 have low values indicative of shielding from solvent. These data and nuclear Overhauser enhancements between protons widely separated in the primary structure suggest a compact structure for the peptide in dimethyl sulfoxide, probably associated with a reverse turn about the Gly4Ala5 residues. In freshly prepared solutions in the concentration range 0.20-5.0 mM, effects of intermolecular aggregation are not observed, but such aggregation may occur under other conditions.