4b2a
From Proteopedia
(Difference between revisions)
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b2a RCSB], [http://www.ebi.ac.uk/pdbsum/4b2a PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b2a RCSB], [http://www.ebi.ac.uk/pdbsum/4b2a PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Abstract The energetics of macromolecular interactions are complex, particularly where protein flexibility is involved. Exploiting serendipitous differences in the plasticity of a series of closely related trypsin variants, we analyzed the enthalpic and entropic contributions accompanying interaction with L45K-eglin C. Binding of the four variants show significant differences in released heat, although the affinities vary little, in accordance with the principle of enthalpy-entropy compensation. Binding of the most disordered variant is almost entirely enthalpically driven, with practically no entropy change. As structures of the complexes reveal negligible differences in protein-inhibitor contacts, we conclude that solvent effects contribute significantly to binding affinities. | ||
| + | |||
| + | Thermodynamic signatures in macromolecular interactions involving conformational flexibility.,Menzel A, Neumann P, Schwieger C, Stubbs MT Biol Chem. 2014 Jul 1;395(7-8):905-11. doi: 10.1515/hsz-2014-0177. PMID:25003391<ref>PMID:25003391</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Eglin|Eglin]] | *[[Eglin|Eglin]] | ||
*[[Trypsin|Trypsin]] | *[[Trypsin|Trypsin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:40, 23 July 2014
Structure of the factor Xa-like trypsin variant triple-Ala (TGA) in complex with eglin C
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