Abstract
THE hydrophobic bond is the term used by Kauzmann1 to describe the gain in free energy on the transfer of non-polar residues from an aqueous environment to the interior of proteins. This has been accepted as one of the major forces involved in the folding of proteins. The exact origin of the energy of the hydrophobic bond is controversial2, but empirical values have been derived for 10 protein residue side chains by Nozaki and Tanford3 who measured the solubility of amino acids in the organic solvents ethanol and dioxane.
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References
Kauzmann, W., Advances in Protein Chemistry, 14, 1 (1959).
Klapper, M. H., Progress in Biorganic Chemistry, 2, 55 (1973).
Nozaki, Y., and Tanford, C., J. biol. Chem., 246, 2211 (1971).
Lee, B., and Richards, F. M., J. molec. Biol., 55, 379 (1971).
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Kauzmann, W., in The Mechanism of Enzyme Action (Johns Hopkins University Press, Baltimore, 1954).
Hermann, R. B., J. phys. Chem., Ithaca., 76, 2754 (1972).
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CHOTHIA, C. Hydrophobic bonding and accessible surface area in proteins. Nature 248, 338–339 (1974). https://doi.org/10.1038/248338a0
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DOI: https://doi.org/10.1038/248338a0
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