THERMODYNAMIC PARAMETERS OF TRANSFER OF N‐ACETYL ETHYL ESTERS OF DIFFERENT AMINO ACIDS FROM ORGANIC SOLVENTS TO WATER
- 1 May 1976
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 8 (3) , 253-264
- https://doi.org/10.1111/j.1399-3011.1976.tb02501.x
Abstract
The distribution coefficients of N-acetyl ethyl esters of glycine, diglycine, β-alanine, alanine, valine, norvaline, leucine and norleucine between water and different organic solvents have been measured at different temperatures. Similar distribution coefficients have been measured for simple amides, urea, formamide, acetamide and N-methyl acetamide. From the distribution measurements, ΔGtr, the free energy of transfer of the solutes from organic solvents to water has been calculated. The temperature dependence of the distribution coefficient values has been utilised to determine the enthalpy of transfer, ΔHtr, and entropy of transfer ΔStr for the above process. From these results similar thermodynamic parameters for the transfer of different nonpolar side chains and peptide groups have been determined and compared with the available data in the literature.This publication has 16 references indexed in Scilit:
- Interaction of amino acids, N-acetyl amino acid esters, thymine and adenine with sephadex LH-20 gelJournal of Chromatography A, 1975
- Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residuesArchives of Biochemistry and Biophysics, 1974
- Model studies on the effects of neutral salts on the conformational stability of biological macromolecules. II. Effects of vicinal hydrophobic groups on the specificity of binding of ions to amide groupsBiochemistry, 1973
- Effects of salts on the free energy of the peptide groupJournal of the American Chemical Society, 1972
- Thermodynamic basis of induced fit. Specific alkane binding to proteinsBiochemistry, 1969
- Thermodynamics of transfer of amides from an apolar to an aqueous solutionBiochemistry, 1969
- Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of ProteinsJournal of the American Chemical Society, 1962
- Hydrogen Bonds between Model Peptide Groups in SolutionJournal of the American Chemical Society, 1962
- Near Infrared Spectra of Compounds with Two Peptide Bonds and the Configuration of a Polypeptide Chain. IIIJournal of the American Chemical Society, 1953
- PROTEINS, AMINO ACIDS AND PEPTIDES as Ions and Dipolar IonsThe Lancet Healthy Longevity, 1943