5io5 | pdb_00005io5

Unliganded form of bovine beta-lactoglobulin, ambient pressure

spinqualitylabelsall models 5io5, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5io5 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactoglobulin 3D structures

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