Alcohol induced conformational transitions of proteins and polypeptides. Thermodynamic studies of some model compounds.

Abstract

Integral enthalpies of solution of diglycine in tert.-butyl alcohol + water and of diglycine and beta-alanine in ethanol + water mixtures were measured at 298.15 K as a function of alcohol concentration. Enthalpies of transfer of the solutes from water to aqueous alcohol mixtures were evaluated from these data. Entropies of transfer of a peptide backbone unit (CH2CONH) and peptide group (CONH) from water to aqueous ethanol solutions were derived from the enthalpy of transfer data and the free energies of transfer of glycine, alpha-alanine, beta-alanine and diglycine. The thermodynamic transfer functions are discussed in terms of "water structure" mediated solute-solute interactions. The observed trends in the thermodynamic transfer functions have also been utilized to rationalize the effect of alcohols on the conformational stability of proteins and polypeptides in aqueous solutions.