Thermodynamics of solvation of proteins in guanidine hydrochloride

✍ Scribed by Faizan Ahmad; Charles C. Bigelow

• Publisher: Wiley (John Wiley & Sons)
• Year: 1990
• Tongue: English
• Weight: 478 KB
• Volume: 29
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360291209

✦ Synopsis

Abstract

The interpretation of the thermodynamic quantities of solvation, that is, Gibbs free energy, enthalpy, and entropy changes for the transfer of proteins from water to 6__M__ guanidine hydrochloride, in terms of the thermodynamic transfer parameters of the groups that make up the protein molecule, is unsatisfactory. We believe this is because the latter are assumed to be identical to the transfer parameters of similar groups attached to smaller model compounds (amino acids and dipeptides). We have empirically determined relationships between transfer quantities for individual protein components and similar groups in model compounds. Comparison of calculated values, based on the modified theory, with the experimental values, reveals very good agreement.