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        <identifier>oai:www.ideals.illinois.edu:2142/84121</identifier>
        <datestamp>2023-07-11</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>Kenneth S. Suslick</dc:contributor>
          <dc:creator>Wang, Jiangyun</dc:creator>
          <dc:date>2015-09-25T22:13:02Z</dc:date>
          <dc:date>2015-09-25T22:13:02Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>2003</dc:date>
          <dc:date>2003</dc:date>
          <dc:description>"We have developed an interesting hypothesis for Olfactory Receptor (OR) mechanism. We are so sensitive to thiols and amines that the most natural way to explain this is that OR is a metalloprotein. We have found a consensus sequence ""HXXCE"" in the 4--5 loop of ORs, which not only binds strongly to Cu2+ and Zn2+, but also turns alpha helical after metal binding. Since the 4--5 loop is as hydrophobic as the fourth helix of OR, charge neutralization of metal ion increases its hydrophobicity, thus it might turn into transmembrane helix and replace the fourth helix. Endogenous ligand binding to the metal site might disturb the charge balance and triggers helix motion, which results in a cell signaling cascade, and eventually the sense of smell."</dc:description>
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  Previous issue date: 2003</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 85402
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>191 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.</dc:description>
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          <dc:language>eng</dc:language>
          <dc:subject>Chemistry, Biochemistry</dc:subject>
          <dc:title>De Novo Heme Protein Design</dc:title>
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            <department>Chemistry</department>
            <discipline>Chemistry</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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