Show simple item record

dc.contributor.supervisor Wieden, Hans-Joachim
dc.contributor.author Mercier, Evan A.
dc.date.accessioned 2014-07-21T18:40:09Z
dc.date.available 2014-07-21T18:40:09Z
dc.date.issued 2013
dc.identifier.uri https://hdl.handle.net/10133/3465
dc.description xii, 235 leaves : ill. (some col.) ; 29 cm en_US
dc.description.abstract Elongation Factor (EF) Tu is universally conserved and delivers aminoacyl-tRNAs (aatRNAs) to the ribosome. To perform this essential task, EF-Tu binds aa-tRNA in an active GTP-bound state, and GTP hydrolysis is critical for deposition of aa-tRNA into the ribosome. Following each aa-tRNA delivery, nucleotide exchange is required for reactivation of EF-Tu•GDP to EF-Tu•GTP. EF-Tu undergoes a variety of conformational changes during each round of aa-tRNA delivery and reactivation. Here, molecular dynamics simulations in silico and kinetic measurements in vitro demonstrate that structural dynamics of EF-Tu on the sub-nanosecond timescale are correlated with EF-Tu functions on the timescale of seconds. Specifically, structural dynamics of the conserved P-loop and switch II regions are important for nucleotide binding in EF-Tu. Additionally, interactions between domain II of EF-Tu and the small ribosomal subunit, which stimulate GTP hydrolysis on EF-Tu, have the potential to regulate structural dynamics of switch I and switch II. en_US
dc.language.iso en_CA 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 Genetic translation -- Research en_US
dc.subject Aminoacyl-tRNA -- Research en_US
dc.subject G proteins -- Research en_US
dc.subject Dissertations, Academic en_US
dc.title Structural dynamics of elongation factor Tu 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.proquestyes No en_US


Files in this item

This item appears in the following Collection(s)

Show simple item record