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        <identifier>oai:www.ideals.illinois.edu:2142/34369</identifier>
        <datestamp>2023-07-10</datestamp>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Baranger, Anne M.</dc:contributor>
          <dc:contributor>Baranger, Anne M.</dc:contributor>
          <dc:contributor>Katzenellenbogen, John A.</dc:contributor>
          <dc:contributor>Hergenrother, Paul J.</dc:contributor>
          <dc:contributor>Zhao, Huimin</dc:contributor>
          <dc:creator>Baek, Jung-Un</dc:creator>
          <dc:date>2012-09-18T21:13:39Z</dc:date>
          <dc:date>2012-09-18T21:13:39Z</dc:date>
          <dc:date>2012-08</dc:date>
          <dc:date>2012-09-18T21:13:39Z</dc:date>
          <dc:date>2012-08</dc:date>
          <dc:description>The RNA recognition motif (RRM) is the most abundant RNA binding domain that is
found in all organisms. RRM-containing proteins participate in most steps of gene expression,
including translation, splicing, modification and transport of RNA. This dissertation aims to help
understand the interactions of the RNA recognition motif and RNA by developing a small
molecule modulator of the interaction and analyzing the kinetics of dissociation. The first
chapter gives an introduction to the function and structural characteristics of RNA binding
proteins, RNA recognition motifs and two RRM proteins, U1A and Sex lethal protein. Chapter 2
describes the identification and analysis of three small molecules that disrupt two different
RRM-RNA complexes, Sex lethal protein-tra RNA and U1A-SL2 RNA. The research discussed
in chapter 3 focus on the role of positively charged residues in the U1A protein and SL2 RNA
complex dissociation process. Analysis of kinetics data obtained by temperature jump and
stopped-flow experiments showed that the location of the electrostatic interaction controls the
rate of different steps in the complex dissociation pathway. Chapter 4 is a description of a
simple and rapid method to detect RNA splice variants using biarsenical dyes and split
tetracysteine moieties, which may accelerate biochemical studies of alternative splicing and
identification of factors that modulate RNA splicing.</dc:description>
          <dc:description>Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2012-06-26T14:38:19Z
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University of Illinois Theses &amp; Dissertations (ID: 1)
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          <dc:identifier>http://hdl.handle.net/2142/34369</dc:identifier>
          <dc:language>en</dc:language>
          <dc:rights>Copyright 2012 Jung-Un Baek</dc:rights>
          <dc:subject>RNA binding protein</dc:subject>
          <dc:subject>Small molecule</dc:subject>
          <dc:subject>RNA recognition motif</dc:subject>
          <dc:subject>Kinetics</dc:subject>
          <dc:subject>Protein-RNA interaction</dc:subject>
          <dc:title>Investigation of the interactions in RNA recognition motif-RNA complexes: small molecule inhibitors and kinetics of dissociation</dc:title>
          <degree>
            <department>Chemistry</department>
            <departmentCode>1413</departmentCode>
            <discipline>Chemistry</discipline>
            <disciplineCode>0335</disciplineCode>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
            <program>PHD:Chemistry -UIUC</program>
            <programCode>10KS0335PHD</programCode>
          </degree>
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