5io6: Difference between revisions
New page: ==Bovine beta-lactoglobulin complex with dodecane, ambient pressure== <StructureSection load='5io6' size='340' side='right' caption='5io6, resolution 2.85Å' scene... |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Bovine beta-lactoglobulin complex with dodecane, ambient pressure== | ==Bovine beta-lactoglobulin complex with dodecane, ambient pressure== | ||
<StructureSection load='5io6' size='340' side='right' caption='[[5io6]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='5io6' size='340' side='right'caption='[[5io6]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5io6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5io6]] 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=5IO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IO6 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]] 2.851Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5io6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5io6 OCA], [https://pdbe.org/5io6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5io6 RCSB], [https://www.ebi.ac.uk/pdbsum/5io6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5io6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B5B0D4_BOVIN B5B0D4_BOVIN] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5io6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</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, ambient pressureBovine beta-lactoglobulin complex with dodecane, ambient pressure
Structural highlights
FunctionPublication 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
|
| ||||||||||||||||||