1znk: Difference between revisions

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[[Image:1znk.gif|left|200px]]
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{{STRUCTURE_1znk|  PDB=1znk  |  SCENE=  }}  
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'''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex'''
===Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex===




==Overview==
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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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{{ABSTRACT_PUBMED_16316253}}


==About this Structure==
==About this Structure==
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[[Category: Beta-barrel]]
[[Category: Beta-barrel]]
[[Category: Lipocalin]]
[[Category: Lipocalin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:50:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:31:20 2008''

Revision as of 18:31, 28 July 2008

File:1znk.png

Template:STRUCTURE 1znk

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

Template:ABSTRACT PUBMED 16316253

About this Structure

1ZNK 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

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