<?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>2026-09-20T21:22:13Z</responseDate><request verb="GetRecord" identifier="oai:wakespace.lib.wfu.edu:10339/37251" metadataPrefix="dim">https://wakespace.lib.wfu.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:null:10339/37251</identifier><datestamp>2026-09-02T09:13:52Z</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">Banerjee, Papri</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2012-06-12T08:35:42Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2014-06-12T08:30:07Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2012</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">https://wakespace.lib.wfu.edu/handle/10339/37251</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">Proteins are dynamic macromolecules. According to Koshland&amp;apos;s classical &amp;quot;induced fit&amp;quot; model of enzyme regulation, proteins have essential conformational flexibility for ligand binding, which promotes catalysis by structural rearrangement. Proteins undergo structural rearrangements to bind ligands, regulate access to a catalytic site, or release products. The energetic contribution of protein flexibility to catalysis is not well understood, despite numerous high resolution crystal structures available for numerous proteins bound with their corresponding ligands.</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" />
   <dim:field mdschema="dc" element="title" lang="en_US">Investigating the Role of Conformational Flexibility in tRNA Aminoacylation</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">Cho, Samuel</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">Dos Santos, Patricia</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">2014-06-12</dim:field>
   <dim:field mdschema="others" element="access-status">restricted</dim:field>
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