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Structural and functional dynamics of Escherichia coli ribonuclease II : initial studies using a novel fluorescence based system

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dc.contributor.advisor Mosimann, Steven
dc.contributor.advisor Wieden, Hans-Joachim
dc.contributor.author Smith, Adam David
dc.contributor.author University of Lethbridge. Faculty of Arts and Science
dc.date.accessioned 2011-06-02T19:06:15Z
dc.date.available 2011-06-02T19:06:15Z
dc.date.issued 2009
dc.identifier.uri http://hdl.handle.net/10133/1289
dc.description xii, 90 leaves : ill. (some col.) ; 29 cm en_US
dc.description.abstract Ribonuclease II (RNase II) is a bacterial enzyme responsible for 90% of the exonucleolytic degradation of mRNA in bacteria, and has bacterial homologues known to be involved in virulence. The goal of this project was to examine the structural dynamics of RNase II using fluorescence. Prior to the beginning of this project, little was known regarding the structural composition of RNase II – required information in the study of structural dynamics. Consequently, the structure of RNase II was studied by constructing a series of deletion mutants in order to map the domains. The publication of an atomic resolution structure of RNase II allowed the project to move directly into the study of RNase II structural dynamics as it degrades mRNA. As a step towards this, RNase II was fluorescently labeled, and preliminary binding studies of DNA – a competitive inhibitor – to RNase II using fluorescence were conducted. en_US
dc.language.iso en_US en_US
dc.publisher Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2009 en_US
dc.relation.ispartofseries Thesis (University of Lethbridge. Faculty of Arts and Science) en_US
dc.subject Ribonucleases -- Research en_US
dc.subject Escherichia coli -- Research en_US
dc.subject Messenger RNA -- Research en_US
dc.subject Dissertations, Academic en_US
dc.title Structural and functional dynamics of Escherichia coli ribonuclease II : initial studies using a novel fluorescence based system en_US
dc.type Thesis en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biology en_US

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