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| | <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 [http://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 [http://proteopedia.org/fgij/fg.htm?mol=5IO7 FirstGlance]. <br> | + | <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='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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5io5|5io5]], [[5io6|5io6]]</td></tr> | + | <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'>[http://proteopedia.org/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> | + | <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 == |
| - | [[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. | + | [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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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Biela, A]] | + | [[Category: Biela A]] |
| - | [[Category: Kurpiewska, K]] | + | [[Category: Kurpiewska K]] |
| - | [[Category: Beta-lactoglobulin]]
| + | |
| - | [[Category: Lipocalin]]
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| - | [[Category: Transport protein]]
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| Structural highlights
Function
LACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kurpiewska K, Biela A, Loch JI, Swiatek S, Jachimska B, Lewinski K. Investigation of high pressure effect on the structure and adsorption of beta-lactoglobulin. Colloids Surf B Biointerfaces. 2017 Oct 31;161:387-393. doi:, 10.1016/j.colsurfb.2017.10.069. PMID:29112912 doi:http://dx.doi.org/10.1016/j.colsurfb.2017.10.069
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