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        <identifier>oai:www.ideals.illinois.edu:2142/82423</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_5131</setSpec>
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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>Leckband, Deborah E.</dc:contributor>
          <dc:creator>Maruthamuthu, Venkat</dc:creator>
          <dc:date>2015-09-25T20:43:58Z</dc:date>
          <dc:date>2015-09-25T20:43:58Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>2009</dc:date>
          <dc:date>2009</dc:date>
          <dc:description>NCAM forms a complex between its terminal domains Ig1 and Ig2. When NCAM of cell A and cell B connect to each other through complexes Ig12(A)/Ig12(B), the relative mobility of cells A and B and membrane tension exerts a force on the Ig12(A)/Ig12(B) complex. Here we investigate the response of the complex to force, using steered molecular dynamics. Starting from the structure of the complex from the Ig1-Ig2-Ig3 fragment, we first equilibrate the complex in solvent and show that its actual end-to-end length is markedly larger than in the crystal structure. We then show that the Ig12/Ig12 complex can behave as a molecular spring of spring constant &amp;sim;0.03 N/m in response to forces of tens of pico-Newton. Such tertiary structure elasticity can be expected to be pervasive considering the large number of multi-modular CAMs. Finally, we rupture the complex using higher forces to identify E16, F19, K98, and L175 as key residues stabilizing the complex.</dc:description>
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  Previous issue date: 2009</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 83704
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>151 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/82423</dc:identifier>
          <dc:identifier>(MiAaPQ)AAI3363031</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Chemistry, Biochemistry</dc:subject>
          <dc:title>Molecular Mechanisms of Cell Adhesion</dc:title>
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          <degree>
            <department>Chemical Engineering</department>
            <discipline>Chemical Engineering</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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