Strong Solute−Solute Dispersive Interactions in a Protein−Ligand Complex
- 11 November 2005
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 127 (48), 17061-17067
- https://doi.org/10.1021/ja055454g
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.Keywords
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