## 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
Thermodynamic analysis of “preferential solvation” in protein solutions
✍ Scribed by Peter R. Wills; Donald J. Winzor
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1993
- Tongue
- English
- Weight
- 266 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
To understand water-protein interactions in solution, the electrostatic field is calculated by solving the Poisson-Boltzmann equation, and the free energy surface of water is mapped by translating and rotating an explicit water molecule around the protein. The calculation is applied to T4 lysozyme w
## Studies on the solvatochromic behaviour of N-methyl-4-and N-methyl-2-[(4-dimethylaminophenyl)iminomethyl]pyr- idinium iodide dyes in a variety of solvents and the preferential solvation of the former dye in binary mixtures of protic and non-protic solvents are presented and interpreted in terms
A methodology using biosensor technology for combined kinetic and thermodynamic analysis of biomolecular interactions is described. Rate and affinity constants are determined with BIAcore. Thermodynamics parameters, changes in free energy, enthalpy and entropy, are evaluated from equilibrium data an
Dissociation constants (pK a ) of trazodone hydrochloride (TZD ¥ HCl) in EtOH/H 2 O media containing 0, 10, 20, 30, 40, 50, 60, 70, and 80% (v/v) EtOH at 288.15, 298.15, 308.15, and 318.15 K were determined by potentiometric techniques. At any temperature, pK a decreased as the solvent was enriched