Alcohol induced conformational transitions of proteins and polypeptides

Mishra, A. K. ; Ahluwalia, J. C. (1983) Alcohol induced conformational transitions of proteins and polypeptides International Journal of Peptide and Protein Research, 21 (3). pp. 322-330. ISSN 0367-8377

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Integral enthalpies of solution of diglycine in tert-butyl alcohol + water and of diglycine and β-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, α-alanine, β-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

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons, Inc.
Keywords:Conformational Transitions of Proteins and Polypeptides ; Denaturation of Proteins by Alcohols ; Enthalpy of Transfer of Diglycine and β-alanine ; Entropy of Transfer of the Peptide Group ; Thermodynamics of Peptides in Solution
ID Code:318
Deposited On:21 Sep 2010 04:50
Last Modified:11 May 2011 07:18

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