Moeser, Beate and Horinek, Dominik (2015) The role of the concentration scale in the definition of transfer free energies. BIOPHYSICAL CHEMISTRY, 196. pp. 68-76. ISSN 0301-4622, 1873-4200
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The Gibbs free energy of transferring a solute at infinite dilution between two solvents quantifies differences in solute-solvent interactions if the transfer takes place at constant molarity of the solute. Yet, many calculation formulae and measuring instructions that are commonly used to quantify solute-solvent interactions correspond to transfer processes in which not the molarity of the solute but its concentration measured in another concentration scale is constant. Here, we demonstrate that in this case, not only the change in solute-solvent interactions is quantified but also the entropic effect of a volume change during the transfer. Consequently, the "phenomenon" which is known as "concentration-scale dependence" of transfer free energies is simply explained by a volume-entropy effect. Our explanations are of high importance for the study of cosolvent effects on protein stability. (C) 2014 Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | AQUEOUS UREA SOLUTIONS; AMINO-ACIDS; PROTEIN DENATURATION; GLYCINE BETAINE; TRANSFER MODEL; SOLUBILITY; STABILITY; OSMOLYTE; BACKBONE; Transfer free energy; Concentration scale; Solute-solvent interaction; Cosolvent and osmolyte effects on proteins; Preferential interaction; Thermodynamics of solvation |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry) > Prof. Dr. Dominik Horinek |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 05 Aug 2019 07:41 |
| Last Modified: | 05 Aug 2019 07:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/6388 |
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