Role of hydrophobicity in protein structure is overestimated
- 1 November 1989
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 34 (5) , 405-408
- https://doi.org/10.1111/j.1399-3011.1989.tb00709.x
Abstract
Some microcalorimetrically measured and theoretically calculated thermodynamic interaction coefficients of amino acid compounds in aqueous and peptidic systems have been collected, and are reported here. They indicate that although hydrophobicity contributes to the stability of the native structure of proteins, its influence on their exact configuration is limited.Keywords
This publication has 27 references indexed in Scilit:
- A study of solute-solute interactions of amides dissolved in N-methylformamide by enthalpic interaction coefficientsJournal of Solution Chemistry, 1988
- The accessible surface area and stability of oligomeric proteinsNature, 1987
- Thermodynamics of unfoldingNature, 1987
- Local sequence patterns of hydrophobicity and solvent accessibility in soluble globular proteinsBiopolymers, 1987
- Temperature dependence of the hydrophobic interaction in protein folding.Proceedings of the National Academy of Sciences, 1986
- Aqueous solutions containing amino acids and peptides. Part 24.—Free energetic and enthalpic coefficients for the interactions of some prolyl and sarcosyl terminally substituted compounds at 25 °CJournal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases, 1986
- Solvation energy in protein folding and bindingNature, 1986
- Prediction of secondary structure of proteins by means of hydrophobicity profilesFEBS Letters, 1982
- Aqueous solutions containing amino acids and peptides. Part 11.—Enthalpy of dilution of single and binary solute solutions of N-acetylglycine amide, N-acetyl-L-alanine amide, N-acetyl-L-valine amide and N-acetyl-L-leucine amide at 298.15 KJournal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases, 1980
- Some Factors in the Interpretation of Protein DenaturationAdvances in Protein Chemistry, 1959