4b1t: 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=4b1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b1t RCSB], [http://www.ebi.ac.uk/pdbsum/4b1t PDBsum]</span></td></tr>
 <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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
 ==See Also==
 *[[Eglin|Eglin]]
 *[[Trypsin|Trypsin]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>