The interaction in water of cyclomaltohexaose (a-cyclodextrin) with monocarboxylic acids from C 3 to C12 has been studied calorimetrically at 25 °C in phosphate buffer, pH 11.3. When a complex forms, calorimetry enables the calculation of both the enthalpy and the association constant, from which th
Thermodynamic interaction between urea and the peptide group in aqueous solutions at 25°C
✍ Scribed by Hansjürgen Schönert; Leo Stroth
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 512 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Isopiestic vapor pressure measurements of the ternary systems water + triglycine + urea and water + glycine‐L‐alanine + urea were made and used to calculate the Gibbs free energy of these systems. Together with recently published analogous results on systems, in which the first solute was glycine or alanine or diglycine, and measurements of the excess enthalpy of all these solutions, it is possible to calculate the Gibbs free energy of transfer and the enthalpy of transfer of the peptide group from water to aqueous urea solutions. The transfer can be described as a binding of urea to the peptide group with Δ__G__ = −1.85 kJ mol^−1^ and Δ__H__ = −18.7 kJ mol^−1^ at 298.1 K.
📜 SIMILAR VOLUMES
The interaction in water of a-and /3-cyclodextrins with L-phenylalanine, L-tyrosine, L-tryptophan, and L-histidine has been studied calorimetrically at 25°C in pure water and in a phosphate buffer (pH 11.3). The interaction in water of a-cyclodextrin with some a, to-amino acids was also studied. Whe