1znl: Difference between revisions

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[[Image:1znl.~~gif~~|left|200px]]

[[Image:1znl.png|left|200px]]

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16316253}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16316253 is the PubMed ID number.

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==About this Structure==

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[[Category: Decan-1-ol]]

[[Category: Lipocalin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 17~~:50:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:29:35 2008''

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-[[Image:1znl.gif|left|200px]]
+{{Seed}}
+[[Image:1znl.png|left|200px]]
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 {{STRUCTURE_1znl|  PDB=1znl  |  SCENE=  }}
-'''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16316253}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16316253 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16316253}}
 ==About this Structure==
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 [[Category: Decan-1-ol]]
 [[Category: Lipocalin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:50:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:29:35 2008''