The hydrophobic effect

B. Widom, P. Bhimalapuram, Kenichiro Koga

    Research output: Contribution to journalReview articlepeer-review

    224 Citations (Scopus)


    The thermodynamics of the hydrophobic effect, as measured primarily through the temperature dependence of solubility, is reviewed, and then a class of models that incorporate the basic mechanism of hydrophobicity is described. These models predict a quantitative relation between the free energy of hydrophobic hydration and the strength of the solvent-mediated attraction between pairs of solute molecules. It is remarked that the free energy of attraction being just of the order of the thermal energy kT may be important for the effective operation of the hydrophobic effect in proteins. Deviations from pairwise additivity of hydrophobic forces are also briefly discussed.

    Original languageEnglish
    Pages (from-to)3085-3093
    Number of pages9
    JournalPhysical Chemistry Chemical Physics
    Issue number15
    Publication statusPublished - Aug 1 2003

    ASJC Scopus subject areas

    • Physics and Astronomy(all)
    • Physical and Theoretical Chemistry


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