Partial molar heat capacities and volumes of Gly-X-Gly tripeptides in aqueous solution: model studies for the rationalization of thermodynamic parameters of proteins
- 31 May 1995
- journal article
- research article
- Published by Elsevier in Biophysical Chemistry
- Vol. 54 (3), 261-269
- https://doi.org/10.1016/0301-4622(94)00131-3
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Analysis of the heat capacity dependence of protein foldingJournal of Molecular Biology, 1992
- Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfoldingJournal of Molecular Biology, 1992
- Partial molar heat capacities of the side chains of some amino acid residues in aqueous solutionBiophysical Chemistry, 1990
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Thermodynamic properties of peptide solutions. Part 6.—The amino acid side-chain contributions to the partial molar volumes and heat capacities of some tripeptides in aqueous solutionJournal of the Chemical Society, Faraday Transactions, 1989
- Stability of Protein Structure and Hydrophobic InteractionAdvances in protein chemistry, 1988
- Solvation of amino acid residues in water and urea-water mixtures: Volumes and heat capacities of 20 amino acids in water and in 8 molar urea at 25 CJournal of Solution Chemistry, 1986
- Thermochemistry of solutions of biochemical model compounds. 4. The partial molar heat capacities of some amino acids in aqueous solutionThe Journal of Chemical Thermodynamics, 1975
- Specific Heat Measurements on Lysozyme, Chymotrypsinogen, and Ovalbumin in Aqueous Solution and in Solid State.Acta Chemica Scandinavica, 1974