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Abstract Recent advances in theoretical and experimental studies of hydrophobic interactions are reviewed. The theory of water structure as applied to hydrophobic bonding, theoretical estimates for the free energy of unfolding of proteins, and the statistical mechanical theory of hydrophobic bonding in polyamino acids are summarized. Experimental estimates of the thermodynamic parameters of the hydrophobic bond can be obtained from solubility and dimerization data of low molecular weight compounds. Recent studies of the interaction of proteins with nonpolar solutes are discussed. Hydrophobic bonds can also be important in various other kinds of interactions involving proteins. The observed effect of urea is mentioned, although no theoretical interpretation of this effect is available yet. In conclusion the methods available for the detection of hydrophobic interactions are reviewed.
George Némethy (1967) studied this question.