Abstract
Several spectroscopic techniques were used to study the states of solvation of the tyrosyls of bovine pancreatic ribonuclease A and tyrosyl model compounds in aqueous 2-methyl-2,4-pentanediol. The wavelength of the tyrosyl peak of the direct spectrum of RNase and the fluorescent quantum efficiency of RNase change little from 0 to 50% methylpentanediol concentration, while for model compounds these properties change markedly. Solvent perturbation difference spectra show very low apparent exposure of tyrosyl. Model compounds show pronounced “magic” mole fraction extrema in thermal perturbation difference spectra, while RNase shows a much smaller effect. The results are interpreted as indicating that the exposed tyrosyl residues of native ribonuclease A in aqueous methylpentanediol are preferentially hydrated relative to the model compounds.
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