Abstract
Large negative standard heat capacity changes (delta CP degree much less than 0) are the hallmark of processes that remove nonpolar surface from water, including the transfer of nonpolar solutes from water to a nonaqueous phase and the folding, aggregation/association, and ligand-binding reactions of proteins [Sturtevant, J. M. (1977) Proc. Natl. Acad. Sci. USA 74, 2236-2240]. More recently, Baldwin [Baldwin, R. L. (1986) Proc. Natl. Acad. Sci. USA 83, 8069-8072] proposed that the delta CP degree of protein folding could be used to quantify the contribution of the burial of nonpolar surface (the hydrophobic effect) to the stability of a globular protein. We demonstrate that identical correlations between the delta CP degree and the change in water-accessible nonpolar surface area (delta Anp) are obtained for both the transfer of nonpolar solutes from water to the pure liquid phase and the folding of small globular proteins: delta CP degree/delta Anp = -(0.28 +/- 0.05) (where delta Anp is expressed in A2 and delta CP degree is expressed in cal.mol-1.K-1; 1 cal = 4.184 J). The fact that these correlations are identical validates the proposals by both Sturtevant and Baldwin that the hydrophobic effect is in general the dominant contributor to delta CP degree and provides a straightforward means of estimating the contribution of the hydrophobic driving force (delta Ghyd degree) to the standard free energy change of a noncovalent process characterized by a large negative delta CP degree in the physiological temperature range: delta Ghyd degree congruent to (80 +/- 10)delta CP degree.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Baldwin R. L. Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8069–8072. doi: 10.1073/pnas.83.21.8069. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Becktel W. J., Schellman J. A. Protein stability curves. Biopolymers. 1987 Nov;26(11):1859–1877. doi: 10.1002/bip.360261104. [DOI] [PubMed] [Google Scholar]
- Chothia C. Hydrophobic bonding and accessible surface area in proteins. Nature. 1974 Mar 22;248(446):338–339. doi: 10.1038/248338a0. [DOI] [PubMed] [Google Scholar]
- Chothia C. The nature of the accessible and buried surfaces in proteins. J Mol Biol. 1976 Jul 25;105(1):1–12. doi: 10.1016/0022-2836(76)90191-1. [DOI] [PubMed] [Google Scholar]
- Gill S. J., Wadsö I. An equation of state describing hydrophobic interactions. Proc Natl Acad Sci U S A. 1976 Sep;73(9):2955–2958. doi: 10.1073/pnas.73.9.2955. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hvidt A. Interactions of water with nonpolar solutes. Annu Rev Biophys Bioeng. 1983;12:1–20. doi: 10.1146/annurev.bb.12.060183.000245. [DOI] [PubMed] [Google Scholar]
- Kellis J. T., Jr, Nyberg K., Sali D., Fersht A. R. Contribution of hydrophobic interactions to protein stability. Nature. 1988 Jun 23;333(6175):784–786. doi: 10.1038/333784a0. [DOI] [PubMed] [Google Scholar]
- Lee B., Richards F. M. The interpretation of protein structures: estimation of static accessibility. J Mol Biol. 1971 Feb 14;55(3):379–400. doi: 10.1016/0022-2836(71)90324-x. [DOI] [PubMed] [Google Scholar]
- Matsumura M., Becktel W. J., Matthews B. W. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature. 1988 Aug 4;334(6181):406–410. doi: 10.1038/334406a0. [DOI] [PubMed] [Google Scholar]
- Moses E., Hinz H. J. Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters. J Mol Biol. 1983 Nov 5;170(3):765–776. doi: 10.1016/s0022-2836(83)80130-2. [DOI] [PubMed] [Google Scholar]
- Ooi T., Oobatake M., Némethy G., Scheraga H. A. Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. Proc Natl Acad Sci U S A. 1987 May;84(10):3086–3090. doi: 10.1073/pnas.84.10.3086. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pfeil W., Privalov P. L. Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride. Biophys Chem. 1976 Jan;4(1):33–40. doi: 10.1016/0301-4622(76)80004-x. [DOI] [PubMed] [Google Scholar]
- Privalov P. L., Gill S. J. Stability of protein structure and hydrophobic interaction. Adv Protein Chem. 1988;39:191–234. doi: 10.1016/s0065-3233(08)60377-0. [DOI] [PubMed] [Google Scholar]
- Privalov P. L., Khechinashvili N. N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol. 1974 Jul 5;86(3):665–684. doi: 10.1016/0022-2836(74)90188-0. [DOI] [PubMed] [Google Scholar]
- Privalov P. L. Stability of proteins: small globular proteins. Adv Protein Chem. 1979;33:167–241. doi: 10.1016/s0065-3233(08)60460-x. [DOI] [PubMed] [Google Scholar]
- Privalov P. L. Thermodynamic problems of protein structure. Annu Rev Biophys Biophys Chem. 1989;18:47–69. doi: 10.1146/annurev.bb.18.060189.000403. [DOI] [PubMed] [Google Scholar]
- Privalov P. L., Tiktopulo E. I., Venyaminov SYu, Griko YuV, Makhatadze G. I., Khechinashvili N. N. Heat capacity and conformation of proteins in the denatured state. J Mol Biol. 1989 Feb 20;205(4):737–750. doi: 10.1016/0022-2836(89)90318-5. [DOI] [PubMed] [Google Scholar]
- Reynolds J. A., Gilbert D. B., Tanford C. Empirical correlation between hydrophobic free energy and aqueous cavity surface area. Proc Natl Acad Sci U S A. 1974 Aug;71(8):2925–2927. doi: 10.1073/pnas.71.8.2925. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rose G. D., Geselowitz A. R., Lesser G. J., Lee R. H., Zehfus M. H. Hydrophobicity of amino acid residues in globular proteins. Science. 1985 Aug 30;229(4716):834–838. doi: 10.1126/science.4023714. [DOI] [PubMed] [Google Scholar]
- Schellman J. A. The thermodynamic stability of proteins. Annu Rev Biophys Biophys Chem. 1987;16:115–137. doi: 10.1146/annurev.bb.16.060187.000555. [DOI] [PubMed] [Google Scholar]
- Sturtevant J. M. Heat capacity and entropy changes in processes involving proteins. Proc Natl Acad Sci U S A. 1977 Jun;74(6):2236–2240. doi: 10.1073/pnas.74.6.2236. [DOI] [PMC free article] [PubMed] [Google Scholar]