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dc.contributor.authorWang, Honglei
dc.date.accessioned2014-03-04T02:48:34Z
dc.date.available2014-03-04T02:48:34Z
dc.date.issued2007-08
dc.identifier.otherwang_honglei_200708_phd
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/wang_honglei_200708_phd
dc.identifier.urihttp://hdl.handle.net/10724/24310
dc.description.abstractIn all kingdoms of life, proteins synthesis is carried out by the ribosome. Nascent chains leave the ribosome through a narrow tunnel in the large subunit, 50S. In bacteria, the first protein to interact with newly synthesized polypeptides is a ribosome-associated chaperone, trigger factor. The function of trigger factor on the ribosome has been well studied, but little is know the role of unbound trigger factor. Research in this thesis focuses on two proteins, trigger factor and tryptophanase, and their relationship. Tryptophanase was identified as a specific substrate of trigger factor using the two dimensional electrophoresis. Part of tryptophanase was found missing in tig-deletion E. coli strain. In vitro refolding experiment indicated that the recovered activity of tryptophanase can be improved 3 times with trigger factor. This indicates the potential function of trigger factor to facilitate the assembly of tryptophanase tetramer.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectTwo Dimensional Electrophoresis
dc.subjectRibosome
dc.subjectProtein Synthesis
dc.subjectMolecular Chaperone
dc.subjectProtein Refolding
dc.titleIdentifying trigger factor functions and substrates
dc.typeDissertation
dc.description.degreePhD
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorRobert Scott
dc.description.committeeRobert Scott
dc.description.committeeJeffrey Urbauer
dc.description.committeeJonathan Amster


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