A NMR Study of Individual Residues of Proteins in a Random Coil State

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2SS[6-127, 64-80] variant of lysozyme which has two disulfide bridges and lacks the other two disulfide bridges was quite unstructured in water, but a part of the polypeptide chain was gradually frozen into a native-like conformation with increasing glycerol concentration. It was monitored from the protection factors of amide hydrogens against H/D exchange by means of NMR spectroscopy. With increasing glycerol concentration, some selected regions were further protected. The highly protected residues were included in A-, Band C-helices and β3-strand, and especially centered on Ile 55 and Leu 56. In 2SS[6-127, 64-80], long-range interactions were recovered due to the preferential hydration by glycerol in the hydrophobic box of the α-domain.