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  • Title: Strong solute-solute dispersive interactions in a protein-ligand complex.
    Author: Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW.
    Journal: J Am Chem Soc; 2005 Dec 07; 127(48):17061-7. PubMed ID: 16316253.
    Abstract:
    The contributions of solute-solute dispersion interactions to binding thermodynamics have generally been thought to be small, due to the surmised equality between solute-solvent dispersion interactions prior to the interaction versus solute-solute dispersion interactions following the interaction. The thermodynamics of binding of primary alcohols to the major urinary protein (MUP-I) indicate that this general assumption is not justified. The enthalpy of binding becomes more favorable with increasing chain length, whereas the entropy of binding becomes less favorable, both parameters showing a linear dependence. Despite the hydrophobicity of the interacting species, these data show that binding is not dominated by the classical hydrophobic effect, but can be attributed to favorable ligand-protein dispersion interactions.
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