1znl: Difference between revisions
New page: left|200px<br /><applet load="1znl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1znl, resolution 1.7Å" /> '''Strong Solute-Solute ... |
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[[Image:1znl.gif|left|200px]]<br /><applet load="1znl" size=" | [[Image:1znl.gif|left|200px]]<br /><applet load="1znl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1znl, resolution 1.7Å" /> | caption="1znl, resolution 1.7Å" /> | ||
'''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex'''<br /> | '''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex'''<br /> | ||
==Overview== | ==Overview== | ||
The contributions of solute-solute dispersion interactions to binding | 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== | ==About this Structure== | ||
1ZNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CD and DE1 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1ZNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=DE1:'>DE1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barratt, E.]] | [[Category: Barratt, E.]] | ||
[[Category: Bingham, R | [[Category: Bingham, R J.]] | ||
[[Category: Homans, S | [[Category: Homans, S W.]] | ||
[[Category: Johnstone, S.]] | [[Category: Johnstone, S.]] | ||
[[Category: Laughton, C | [[Category: Laughton, C A.]] | ||
[[Category: Malham, R.]] | [[Category: Malham, R.]] | ||
[[Category: Phillips, S | [[Category: Phillips, S E.]] | ||
[[Category: CD]] | [[Category: CD]] | ||
[[Category: DE1]] | [[Category: DE1]] | ||
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[[Category: lipocalin]] | [[Category: lipocalin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:23 2008'' | ||
Revision as of 14:17, 21 February 2008
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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
1ZNL is a Single protein structure of sequence from Mus musculus with CD and DE1 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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