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dc.contributor.supervisor Wieden, Hans-Joachim
dc.contributor.author Brandon, Harland Edward
dc.contributor.author University of Lethbridge. Faculty of Arts and Science
dc.date.accessioned 2021-09-02T16:36:25Z
dc.date.available 2021-09-02T16:36:25Z
dc.date.issued 2021
dc.identifier.uri https://hdl.handle.net/10133/6013
dc.description.abstract Antibiotic resistance is becoming an increasing global health concern. The bacterial protein synthesis machinery, including the ribosome and its associated factors, are the target of over half of the clinically relevant antibiotics currently in use, highlighting the importance of cellular protein production as antibiotic target. The ribosome associated factors HflX and YchF are members of the GTPase superfamily. Their cellular functions are only poorly understood. The overarching goal of this thesis was to determine the location where HflX and YchF bind on the bacterial ribosome. Data presented here confirm that YchF interacts with the ribosomal A-site, while HflX is unique within the GTPase family being able to bind to both the ribosomal A-site and E-site. From this data and subsequent biochemical and biophysical studies, a mechanism for both HflX and YchF function during protein synthesis, specifically under stress conditions, is proposed. en_US
dc.language.iso en_US 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 HflX en_US
dc.subject YchF en_US
dc.subject bacterial ribosome en_US
dc.subject protein synthesis en_US
dc.subject antibiotic resistance mechanisms en_US
dc.subject NTPases en_US
dc.subject Drug resistance in microorganisms -- Research en_US
dc.subject Bacterial proteins -- Synthesis -- Research en_US
dc.subject Ribosomes -- Research en_US
dc.subject Ribosomes -- Structure en_US
dc.subject Guanosine triphosphatase en_US
dc.subject Adenosine triphosphatase en_US
dc.subject Dissertations, Academic en_US
dc.title Biophysical studies of 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 Ph.D en_US
dc.proquest.subject 0487 en_US
dc.proquest.subject 0786 en_US
dc.proquestyes Yes en_US


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