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dc.contributor.authorFlora, Kulwinder.en_US
dc.date.accessioned2009-07-09T17:35:32Z
dc.date.available2009-07-09T17:35:32Z
dc.date.issued1998-07-09T17:35:32Z
dc.identifier.urihttp://hdl.handle.net/10464/1884
dc.description.abstractThe successful development of stable biosensors incorporating entrapped proteins suffers from poor understanding of the properties of the entrapped biomolecules. This thesis reports on the use of fluorescence spectroscopy to investigate the properties of proteins entrapped in sol-gel processed silicate materials. Two different single tryptophan (Trp) proteins were investigated in this thesis, the Ca2 + binding protein cod III parvalbumin (C3P) and the salicylate binding protein human serum albumin (HSA). Furthermore, the reactive single cysteine (Cys) residue within C3P and HSA were labelled with the probes iodoacetoxynitrobenzoxadiazole (C3P) and acrylodan (C3P and HSA) to further examine the structure, stability and function of the free and entrapped proteins. The results show that both C3P and HSA can be successfully entrapped into sol-gelderived matrices with retention of function and conformational flexibility.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectFluorimetry.en_US
dc.subjectProteins.en_US
dc.subjectColloids.en_US
dc.titleFluorometric monitoring of the properties of proteins entrapped in sol-gel derived matricesen_US
dc.typeElectronic Thesis or Dissertationen_US
dc.degree.nameM.Sc. Chemistryen_US
dc.degree.levelMastersen_US
dc.contributor.departmentDepartment of Chemistryen_US
dc.degree.disciplineFaculty of Mathematics and Scienceen_US


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