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dc.contributor.supervisor Wieden, Hans-Joachim
dc.contributor.author Coatham, Mackenzie Leigh
dc.date.accessioned 2014-10-14T20:54:40Z
dc.date.available 2014-10-14T20:54:40Z
dc.date.issued 2014
dc.identifier.uri https://hdl.handle.net/10133/3539
dc.description.abstract The functional roles of the two universally conserved bacterial GTPases, HflX and YchF, are poorly understood. Both proteins associate with 70S ribosomes as well as 30S and 50S ribosomal subunits. Understanding exactly how HflX and YchF interact with the ribosome and nucleotides will be important for the discovery of the in vivo relevant ribosomal complex. Presented in this thesis, is the development of a fluorescence-based system that can be used to monitor the association of HflX to 70S, 50S and 30S. Additionally, as HflX lacks the canonical glutamine that is required for the hydrolysis of GTP and ATP, an examination into how HflX hydrolyzes purine nucleotides was conducted. Furthermore, nucleotide association and dissociation rate constants were determined in the presence of ribosomes for YchF and in the presence and absence of antibiotics for HflX. The results presented here provide additional insight into the enzymatic properties of HflX and YchF. en_US
dc.language.iso en en_US
dc.publisher Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry en_US
dc.relation.ispartofseries Thesis (University of Lethbridge. Faculty of Arts and Science) en_US
dc.subject bacteria en_US
dc.subject enzymatic properties en_US
dc.subject GTPases en_US
dc.subject HflX en_US
dc.subject YchF en_US
dc.title Insight into the universally conserved NTPases HflX and YchF en_US
dc.type Thesis en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.degree.level Masters en_US
dc.degree.level Masters
dc.proquest.subject 0487 en_US
dc.proquest.subject 0786 en_US
dc.proquest.subject 0307 en_US
dc.proquestyes Yes en_US


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