Jagiellonian University Repository

4IB7 : Bovine beta-lactoglobulin (isoform A) in complex with dodecyltrimethylammonium (DTAC)

4IB7 : Bovine beta-lactoglobulin (isoform A) in ...

Show full item record

dc.contributor.author Loch, Joanna [SAP13903467] pl
dc.contributor.author Bonarek, Piotr [SAP11019221] pl
dc.contributor.author Polit, Agnieszka [SAP11016972] pl
dc.contributor.author Świątek, Sylwia pl
dc.contributor.author Dziedzicka-Wasylewska, Marta [SAP11019137] pl
dc.contributor.author Lewiński, Krzysztof [SAP11011257] pl
dc.date.accessioned 2016-06-10T09:48:18Z
dc.date.available 2016-06-10T09:48:18Z
dc.date.created 2013 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/27825
dc.language eng pl
dc.rights Dodaję tylko opis bibliograficzny *
dc.rights.uri *
dc.title 4IB7 : Bovine beta-lactoglobulin (isoform A) in complex with dodecyltrimethylammonium (DTAC) pl
dc.type WorkingPaper pl
dc.description.additional Pbl. w bazie danych : Worldwide Protein Data Bank. Powiązana z artykułem o numerze DOI: 10.1002/jmr.2280 pl
dc.identifier.weblink http://www.rcsb.org/pdb/explore.do?structureId=4IB7 pl
dc.abstract.en Isoforms A (LGB-A) and B (LGB-B) of bovine lactoglobulin, the milk protein, differ in positions 64 (D[LEFT RIGHT ARROW]G) and 118 (V[LEFT RIGHT ARROW]A). Interactions of LGB-A and LGB-B with sodium dodecyl sulfate (SDS), dodecyltrimethylammonium chloride (DTAC) and lauric acid (LA), 12-carbon ligands possessing differently charged polar groups, were investigated using isothermal titration calorimetry and X-ray crystallography, to study the proton linkage phenomenon and to distinguish between effects related to different isoforms and different ligand properties. The determined values of ΔS and ΔH revealed that for all ligands, binding is entropically driven. The contribution from enthalpy change is lower and shows strong dependence on type of buffer that indicates proton release from the protein varying with protein isoform and ligand type and involvement of LA and Asp64 (in isoform A) in this process. The ligand affinities for both isoforms were arranged in the same order, DTAC < LA < SDS, and were systematically lower for variant B. The entropy change of the complexation process was always higher for isoform A, but these values were compensated by changes in enthalpy, resulting in almost identical ΔG for complexes of both isoforms. The determined crystal structures showed that substitution in positions 64 and 118 did not influence the overall structure of LGB complexes. The chemical character of the ligand polar group did not affect the position of its aliphatic chain in protein β-barrel, indicating a major role of hydrophobic interactions in ligand binding that prevailed even with the repulsion between positively charged DTAC and lysine residues located at binding site entrance. pl
dc.subject.en transport protein pl
dc.identifier.doi 10.2210/pdb4ib7/pdb pl
dc.date.accession 2016-06-09 pl
dc.affiliation Wydział Chemii : Zakład Krystalochemii i Krystalofizyki pl
dc.affiliation Wydział Biochemii, Biofizyki i Biotechnologii : Zakład Biochemii Fizycznej pl
dc.subtype none pl
dc.rights.original OTHER; otwarte repozytorium; ostateczna wersja wydawcy; w momencie opublikowania; 0; pl

Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)