Structural dynamics of elongation factor Tu

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dc.contributor.authorMercier, Evan A.
dc.contributor.supervisorWieden, Hans-Joachim
dc.date.accessioned2014-07-21T18:40:09Z
dc.date.available2014-07-21T18:40:09Z
dc.date.issued2013
dc.degree.levelPh.Den_US
dc.descriptionxii, 235 leaves : ill. (some col.) ; 29 cmen_US
dc.description.abstractElongation 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.identifier.urihttps://hdl.handle.net/10133/3465
dc.language.isoen_CAen_US
dc.proquestyesNoen_US
dc.publisherLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistryen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.relation.ispartofseriesThesis (University of Lethbridge. Faculty of Arts and Science)en_US
dc.subjectGenetic translation -- Researchen_US
dc.subjectAminoacyl-tRNA -- Researchen_US
dc.subjectG proteins -- Researchen_US
dc.subjectDissertations, Academicen_US
dc.titleStructural dynamics of elongation factor Tuen_US
dc.typeThesisen_US
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