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dc.contributor.supervisor Wieden, Hans-Joachim
dc.contributor.author Mo, Fan
dc.date.accessioned 2012-07-30T22:20:15Z
dc.date.available 2012-07-30T22:20:15Z
dc.date.issued 2011
dc.identifier.uri https://hdl.handle.net/10133/3107
dc.description x, 85 leaves : ill. (some col.) ; 29 cm en_US
dc.description.abstract During protein synthesis, elongation factor Tu (EF-Tu) delivers aminoacyl-tRNA (aa-tRNA) to the A-site of mRNA-programmed ribosomes in a GTP-dependent manner. To enable future studies on the functional and structural requirement of EF-Tu’s function, a Cysteine-free variant of EF-Tu was constructed suitable for subsequent labelling of the protein and use in kinetic studies. Here, the kinetic properties of three Cysteine-less EF-Tu variants are reported, demonstrating that only the variant with the Alanine substitution in position 81 retains wild-type activity with respect to the interaction with guanine nucleotides, aa-tRNA and the ribosome. To explore a possible tRNA independent pathway for the GTPase activation signal, three residues in domain II of EF-Tu (Arginine 279, Glycine 280, Arginine 283) were mutated; the activity of EF-Tu variants were analyzed. Results suggest that these residues are indeed required for efficient ribosome-dependent stimulation of the GTPase activity of EF-Tu. en_US
dc.language.iso en_US en_US
dc.publisher Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2011 en_US
dc.relation.ispartofseries Thesis (University of Lethbridge. Faculty of Arts and Science) en_US
dc.subject Aminoacyl-tRNA en_US
dc.subject Guanosine triphosphatase en_US
dc.subject Proteins -- Synthesis en_US
dc.subject Binding sites (Biochemistry) en_US
dc.subject Genetic translation en_US
dc.subject Escherichia coli en_US
dc.subject Dissertations, Academic en_US
dc.title Functional role of the conserved amino acids Cysteine 81, Arginine 279, Glycine 280 and Arginine 283 in elongation factor Tu from Escherichia coli 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


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