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• W2037193820 abstract "Two bands in the Raman spectrum of myosin, at 1,304 cm-1 and 1,270 cm-1, are attributable to alpha-helical structure. The first of these, also present in the spectrum of light meromyosin (LMM) but not in that of subfragment-1 (S-1), is assigned to the coiled-coil tail region of myosin; the second, seen in spectra of S-1 or heavy meromyosin (HMM), is largely absent from the spectrum of light meromyosin and is likely to correspond to the alpha-helical segments of the head region. When myosin or LMM aggregates, spectral bands attributable to backbone and sidechain groups sharpen suggesting a reduction in motional freedom. This sharpening is particularly apparent in the 902 cm-1 C--C stretching mode. Mg2+ broadens and shifts the peak at 1,244 cm-1 to 1,237 cm-1 and diminishes the intensity from 1,230 to 1,240 cm-1, changes which appear to be associated the S-1 region. MgPPi produces changes in the 1,300 cm-1 region attributable to alpha-helical regions in coiled-coil structures suggesting that MgPPi affects not only S-1, but also some part of the myosin rod." @default.
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• W2037193820 date "1983-11-01" @default.
• W2037193820 modified "2023-10-05" @default.
• W2037193820 title "Studies of myosin and its proteolytic fragments by laser Raman spectroscopy" @default.
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• W2037193820 doi "https://doi.org/10.1016/s0006-3495(83)84294-5" @default.
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