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PDBsum entry 1znh
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Transport protein
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PDB id
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1znh
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References listed in PDB file
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Key reference
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Title
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Strong solute-Solute dispersive interactions in a protein-Ligand complex.
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Authors
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R.Malham,
S.Johnstone,
R.J.Bingham,
E.Barratt,
S.E.Phillips,
C.A.Laughton,
S.W.Homans.
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Ref.
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J Am Chem Soc, 2005,
127,
17061-17067.
[DOI no: ]
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PubMed id
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Abstract
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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.
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