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Lookup NU author(s): Professor Steve Homans
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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.
Author(s): Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SEV, Laughton CA, Homans SW
Publication type: Article
Publication status: Published
Journal: Journal of the American Chemical Society
ISSN (print): 0002-7863
ISSN (electronic): 1520-5126
Publisher: American Chemical Society
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