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        <identifier>oai:www.ideals.illinois.edu:2142/80576</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>Gratton, Enrico</dc:contributor>
          <dc:creator>Colyer, Ryan Anthony</dc:creator>
          <dc:date>2015-09-25T20:03:08Z</dc:date>
          <dc:date>2015-09-25T20:03:08Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>2008</dc:date>
          <dc:date>2008</dc:date>
          <dc:description>This new hardware was used to observe the conformational dynamics of a calmodulin sample labeled with a FRET pair, and encapsulated within 100nm lipid vesicles. A toolbox of analysis techniques was developed for PTA, and was used to quantitatively describe the transitions and fluctuations of the conformation of calmodulin. Analysis was done in a model-free manner, and also by applying known parameters about the system to extract more specific information. Using the information obtained, a conformational model was developed to describe the dynamic behavior of calmodulin's conformation in terms of its binding with calcium. In addition, measurements conducted in the presence of a peptide derived from Ca2+/calmodulin-dependent protein kinase II were used to examine the properties of calmodulin's conformational dynamics while interacting with its binding targets.</dc:description>
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  Previous issue date: 2008</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 81858
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>94 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/80576</dc:identifier>
          <dc:identifier>(MiAaPQ)AAI3337743</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Biophysics, General</dc:subject>
          <dc:title>Development of a Fluorescence Lifetime Based Method to Detect and Analyze Single Molecule Reactions in Solution</dc:title>
          <dc:type>text</dc:type>
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            <department>Physics</department>
            <discipline>Physics</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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