Strong solute-solute dispersive interactions in a protein-ligand complex |
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Authors: | Malham Richard Johnstone Sarah Bingham Richard J Barratt Elizabeth Phillips Simon E V Laughton Charles A Homans Steve W |
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Institution: | Astbury Centre for Structural Molecular Biology, School of Biochemistry & Molecular Biology, University of Leeds, UK. |
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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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