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Issue 15, 2003
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The hydrophobic effect

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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.

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Publication details

The article was received on 10 Apr 2003, accepted on 04 Jun 2003 and first published on 24 Jun 2003

Article type: Invited Article
DOI: 10.1039/B304038K
Citation: Phys. Chem. Chem. Phys., 2003,5, 3085-3093

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    The hydrophobic effect

    B. Widom, P. Bhimalapuram and K. Koga, Phys. Chem. Chem. Phys., 2003, 5, 3085
    DOI: 10.1039/B304038K

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