Show simple item record

dc.contributor.authorHsu, Yu-Ting
dc.date.accessioned2009-04-28T23:29:23Z
dc.date.availableNO_RESTRICTIONen_US
dc.date.available2009-04-28T23:29:23Z
dc.date.issued2008
dc.identifier.urihttp://hdl.handle.net/10179/771
dc.description.abstractBovine ß-lactoglobulin (ß-Lg) has been studied extensively but there is no clear identification of its biological function. Hydrophobic molecules have been observed binding into the hydrophobic calyx of ß-Lg. By comparison with other members of lipocalin family, it is probable that ß-Lg plays a role of transport of ligands, as ligands also bind into the central cavity of lipocalins. The structurally similar MUP is a pheromone-binding protein; therefore, it is possible that ß-Lg may also fulfil a similar role. This study has begun to test this hypothesis by investigating the interactions between bovine ß-Lg and several small volatile molecules (2-sec-4,5-dihydrothiazole, 3-methyl-2-butenal, 3-methyl-2-buten-1-ol and phenylacetic acid). The interactions between the volatile molecules and ß-Lg were studied by both two-dimensional NMR spectroscopy and X-ray crystallographic methods. TOCSY spectra were recorded for ß-Lg and the complex between ß-Lg and the ligands. The observed chemical shifts in the HN-Ha region are sensitive to the proximity of ligands, and hence chemical shift changes on ligand binding provide information on possible binding sites. It appears that several amino acids with hydrophobic sidechains are affected by interaction with volatile molecules at pH 2.0. The X-ray crystallographic study at pH 8.5 showed that the potential ligand, 2-sec-4,5-dihydrothiazole, may have decomposed into a linear 2-methyl-butanol. The refined structure (R=0.281, Rfree=0.354 for reflections to 2.6 Å resolution) reveals that the potential ligand may bind to the central cavity in a manner similar to the binding of 12-bromodecanoic acid to ß-Lg.en_US
dc.language.isoenen_US
dc.publisherMassey Universityen_US
dc.rightsThe Authoren_US
dc.subjectBovine [beta]-lactoglobulinen_US
dc.subjectMolecular biologyen_US
dc.subject.otherFields of Research::250000 Chemical Sciences::250300 Organic Chemistryen_US
dc.titleThe binding of small volatile molecules by bovine [beta]-lactoglobulin : a thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in Chemistry at Massey Universityen_US
dc.typeThesisen_US
thesis.degree.disciplineChemistryen_US
thesis.degree.levelMastersen_US
thesis.degree.nameMaster of Science (M.Sc.)en_US


Files in this item

Icon
Icon
Icon

This item appears in the following Collection(s)

Show simple item record