<?xml version='1.0' encoding='utf-8'?>
<eprints xmlns='http://eprints.org/ep2/data/2.0'>
  <eprint id='http://eprints.iliauni.edu.ge/id/eprint/1301'>
    <eprintid>1301</eprintid>
    <rev_number>5</rev_number>
    <eprint_status>archive</eprint_status>
    <userid>105</userid>
    <dir>disk0/00/00/13/01</dir>
    <datestamp>2014-02-28 13:40:01</datestamp>
    <lastmod>2014-03-12 15:14:10</lastmod>
    <status_changed>2014-02-28 13:40:01</status_changed>
    <type>article</type>
    <succeeds>989</succeeds>
    <metadata_visibility>show</metadata_visibility>
    <creators>
      <item>
        <name>
          <family>Metreveli</family>
          <given>Nunu</given>
        </name>
        <id>nunu_metreveli@iliauni.edu.ge</id>
      </item>
      <item>
        <name>
          <family>Namicheishvili</family>
          <given>L.O.</given>
        </name>
      </item>
      <item>
        <name>
          <family>Dzhariashvili</family>
          <given>K.K.</given>
        </name>
      </item>
      <item>
        <name>
          <family>Chikvaidze</family>
          <given>E.N.</given>
        </name>
      </item>
      <item>
        <name>
          <family>Mrevlishvili</family>
          <given>G.M.</given>
        </name>
      </item>
    </creators>
    <title>A Microcalorimetric and Electron Spin Resonance Study
of the Influence of UV Radiation on Collagen
</title>
    <ispublished>pub</ispublished>
    <subjects>
      <item>QC</item>
      <item>QH301</item>
    </subjects>
    <divisions>
      <item>ins14</item>
    </divisions>
    <full_text_status>none</full_text_status>
    <abstract>It was demonstrated microcalorimetrically that UV radiation cardinally changed the behavioral pattern
of the temperature dependence of heat capacity of a collagen solution and decreased the enthalpy of collagen
denaturation. It was discovered by electron spin resonance (ESR) that the primary products of UV-irradiated
acid-soluble collagen were atomic hydrogen and the anion radical of acetic acid. The latter, when
exposed to long-wavelength UV light, converted into the methyl radical, which interacted with acetic acid to
produce the acetic acid radical. These free radicals interacted with the collagen molecule, leading to the appearance
of seven superfine components with the split H=1.13 mT in the ESR spectrum. It was assumed that this
spectrum is related to the free radical that occurred in the proline residue of the collagen molecule, which, in
this particular case, was the major defect in the triple helix of collagen that caused instability of the macromolecule.
</abstract>
    <date>2006</date>
    <publication>Biophysics</publication>
    <volume>51</volume>
    <number>1</number>
    <pagerange>29-32</pagerange>
    <refereed>TRUE</refereed>
    <issn>0006-3509</issn>
  </eprint>
</eprints>
