1znh
From Proteopedia
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'''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex''' | '''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex''' | ||
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[[Category: Malham, R.]] | [[Category: Malham, R.]] | ||
[[Category: Phillips, S E.]] | [[Category: Phillips, S E.]] | ||
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Revision as of 14:50, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 17:50:37 2008
