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 |