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        <identifier>oai:www.ideals.illinois.edu:2142/23939</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>Frauenfelder, Hans</dc:contributor>
          <dc:creator>Sauke, Todd Bennet</dc:creator>
          <dc:date>2011-05-18T15:24:48Z</dc:date>
          <dc:date>2011-05-18T15:24:48Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1989</dc:date>
          <dc:description>"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A
photon of visible light absorbed by the protein can break the protein ligand bond. At low
temperatures (&gt; 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin
are non-exponential, having amplitude components that extend over many
orders of magnitude in time. The bound and unbound states of the system have different
spectroscopic signatures and the kinetics of recombination can be measured by monitoring
the time dependence of the absorption spectrum of the sample after photodissociation.
After a period of intense illumination with light, the recombination kinetics slow
down. The proteins are ""pumped"" to longer lived states. After waiting, the system resets,
such that a photodissociation initiates regular, non-pumped, kinetics. I have measured the
kinetics of the ""pumped"" states and the time course of the resetting, at various
temperatures. Physical models, including connections to glass theories, are considered,
and thermodynamic parameters for the various processes involved havebeen determined."</dc:description>
          <dc:description>Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-05-18T15:24:48Z
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  Previous issue date: 1989</dc:description>
          <dc:description>Restriction data tranferred 2014-07-01T11:13:43-05:00
Original Data
Group with Access UIUC Users [automated]
Release Date: none
Reason: Thesis</dc:description>
          <dc:description>Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-05-18T15:24:48Z
Item is restricted indefinitely.</dc:description>
          <dc:description>Thesis</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:identifier>3478197</dc:identifier>
          <dc:identifier>http://hdl.handle.net/2142/23939</dc:identifier>
          <dc:language>en</dc:language>
          <dc:rights>1989 Todd Bennet Sauke</dc:rights>
          <dc:subject>carbonmonoxymyoglobin</dc:subject>
          <dc:subject>myoglobin</dc:subject>
          <dc:subject>protein kinetics</dc:subject>
          <dc:subject>ligand binding kinetics</dc:subject>
          <dc:subject>recombination kinetics</dc:subject>
          <dc:subject>illumination</dc:subject>
          <dc:title>Long lived states induced by extended illumination of carbonmonoxy-myoglobin</dc:title>
          <dc:type>Dissertation / Thesis</dc:type>
          <dc:type>text</dc:type>
          <degree>
            <department>Physics</department>
            <discipline>Physics</discipline>
            <disciplineCode>University of Illinois at Urbana-Champaign</disciplineCode>
            <level>Dissertation</level>
            <name>Ph.D.</name>
          </degree>
        </thesis>
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