5io7: Difference between revisions
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==Bovine beta-lactoglobulin complex with dodecane at high pressure (0.43 GPa)== | ==Bovine beta-lactoglobulin complex with dodecane at high pressure (0.43 GPa)== | ||
<StructureSection load='5io7' size='340' side='right' caption='[[5io7]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='5io7' size='340' side='right'caption='[[5io7]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5io7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5io7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IO7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5io7 OCA], [https://pdbe.org/5io7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5io7 RCSB], [https://www.ebi.ac.uk/pdbsum/5io7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5io7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5io7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5io7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Biela A]] | ||
[[Category: | [[Category: Kurpiewska K]] | ||
Latest revision as of 17:03, 30 August 2023
Bovine beta-lactoglobulin complex with dodecane at high pressure (0.43 GPa)Bovine beta-lactoglobulin complex with dodecane at high pressure (0.43 GPa)
Structural highlights
FunctionLACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedbeta-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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