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Solvent perturbation studies and analysis of protein and model compound data in denaturing organic solvents

1973; Elsevier BV; Volume: 54; Issue: 2 Linguagem: Inglês

10.1016/0003-2697(73)90365-5

1096-0309

Nicholas J. Solli, Theodore T. Herskovits,

Analytical Chemistry and Chromatography

For the study of proteins in the denaturing organic alcohols, methanol, ethanol, 1-propanol, trifluoroethanol, and 2-chloroethanol, and the assessment of the number or fraction of exposed tyrosyl and tryptophyl residues in these solvents by the solvent perturbation method of difference spectroscopy, the molar absorbance difference values, Δϵλ of the N-acetyl ethyl esters of tyrosine and tryptophan have been obtained with 20% dimethylsulfoxide as a perturbant, and are presented in the 350-260 nm region. Solvent perturbation data obtained on apomyoglobin, serum albumin, and ovalbumin in several of these solvents are presented and analyzed for the purpose of illustration of the computation and curve-fitting techniques used, employing the tabulated model compound data of this paper.