<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-20T19:25:45Z</responseDate><request verb="GetRecord" identifier="oai:wakespace.lib.wfu.edu:10339/36429" metadataPrefix="dim">https://wakespace.lib.wfu.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:null:10339/36429</identifier><datestamp>2026-09-02T11:57:34Z</datestamp><setSpec>com_10339_14934</setSpec><setSpec>col_10339_38132</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Casina, Veronica Christine</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2012-01-18T09:35:30Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2011</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">https://wakespace.lib.wfu.edu/handle/10339/36429</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">Cellular enzymes interact with RNA substrates at several key stages in an organism&amp;apos;s life cycle, particularly during the processes of transcription and translation. A more detailed description of enzyme mechanistic features and kinetic parameters is important both for understanding molecular function in general and as possible therapeutic targets. The two classes of RNA-interacting enzymes investigated in the work described here are helicases, which disrupt RNA secondary structure, and aminoacyl-tRNA synthetases, which catalyze the attachment of an amino acid to its cognate tRNA.</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en_US">en</dim:field>
   <dim:field mdschema="dc" element="publisher" lang="en_US">Wake Forest University</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Pre-steady state kinetics</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Prokaryote</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Protein biosynthesis</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">RNA stability</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">steady state kinetics</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">strand displacement</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Kinetic and mutational studies of two RNA-interacting enzymes</dim:field>
   <dim:field mdschema="dc" element="type" lang="en_US">Dissertation</dim:field>
   <dim:field mdschema="thesis" element="contributor" qualifier="committeeChair" lang="en_US">Alexander, Rebecca W.</dim:field>
   <dim:field mdschema="thesis" element="contributor" qualifier="committeeMember" lang="en_US">Hollis, Thomas</dim:field>
   <dim:field mdschema="thesis" element="contributor" qualifier="committeeMember" lang="en_US">Bierbach, Ulrich</dim:field>
   <dim:field mdschema="thesis" element="contributor" qualifier="committeeMember" lang="en_US">Colyer, Christa</dim:field>
   <dim:field mdschema="thesis" element="contributor" qualifier="committeeMember" lang="en_US">King, S. Bruce</dim:field>
   <dim:field mdschema="thesis" element="degree" qualifier="discipline" lang="en_US">Chemistry</dim:field>
   <dim:field mdschema="thesis" element="embargo" qualifier="terms" lang="en_US">forever</dim:field>
   <dim:field mdschema="thesis" element="embargo" qualifier="liftdate">10000-01-01</dim:field>
   <dim:field mdschema="others" element="access-status">restricted</dim:field>
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