5io7: Difference between revisions

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 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5io5|5io5]], [[5io6|5io6]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5io7 OCA], [http://pdbe.org/5io7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5io7 RCSB], [http://www.ebi.ac.uk/pdbsum/5io7 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5io7 OCA], [http://pdbe.org/5io7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5io7 RCSB], [http://www.ebi.ac.uk/pdbsum/5io7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5io7 ProSAT]</span></td></tr>
 </table>
 == Function ==
 [[http://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+beta-Lactoglobulin, being one of the principal whey protein, is of huge importance to the food industry. Temperature/pressure effects on this small protein has been extensively studied by industry. To characterize biochemical properties of beta-lactoglobulin after or during pressurization, a wide range of methods have been used thus far. In this study, for the first time, the pressure-induced conformation of beta-lactoglobulin in the crystal state was determined, at pressure 430 MPa. Changes observed in the high pressure structure correlate with the physico-chemical properties of pressure-treated beta-lactoglobulin obtained from dynamic light scattering, electrophoretic mobility and quartz crystal microbalance with dissipation monitoring measurements. A comparison between the beta-lactoglobulin structures determined at both high and ambient pressure contrasts the stable nature of the protein core and adjacent loop fragments. At high pressure the beta-lactoglobulin structure presents early signs of dimer dissociation, charge and conformational changes characteristic for initial unfolded intermediate as well as a significant modification of the binding pocket volume. Those observations are supported by changes in zeta potential values and results in increase affinity of the beta-lactoglobulin adsorption onto gold surface. Observed pressure-induced structural modifications were previously suggested as an important factor contributing to beta-lactoglobulin denaturation process. Presented studies provide detailed analysis of pressure-associated structural changes influencing beta-lactoglobulin conformation and consequently its adsorption.
+Investigation of high pressure effect on the structure and adsorption of beta-lactoglobulin.,Kurpiewska K, Biela A, Loch JI, Swiatek S, Jachimska B, Lewinski K Colloids Surf B Biointerfaces. 2017 Oct 31;161:387-393. doi:, 10.1016/j.colsurfb.2017.10.069. PMID:29112912<ref>PMID:29112912</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5io7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>