1znh

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Revision as of 05:25, 21 November 2007

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spinqualitylabelsall models 1znh, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex

Overview

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.

About this Structure

1ZNH is a Single protein structure of sequence from Mus musculus with CD and OC9 as ligands. Full crystallographic information is available from OCA.

Reference

Strong solute-solute dispersive interactions in a protein-ligand complex., Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW, J Am Chem Soc. 2005 Dec 7;127(48):17061-7. PMID:16316253

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