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  <eprint id='http://eprints.iliauni.edu.ge/id/eprint/1305'>
    <eprintid>1305</eprintid>
    <rev_number>7</rev_number>
    <eprint_status>archive</eprint_status>
    <userid>105</userid>
    <dir>disk0/00/00/13/05</dir>
    <datestamp>2014-02-28 13:39:52</datestamp>
    <lastmod>2015-04-21 09:16:31</lastmod>
    <status_changed>2014-02-28 13:39:52</status_changed>
    <type>article</type>
    <succeeds>1085</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</given>
        </name>
      </item>
      <item>
        <name>
          <family>Jariashvili</family>
          <given>K</given>
        </name>
      </item>
      <item>
        <name>
          <family>Chikvaidze </family>
          <given>E</given>
        </name>
      </item>
      <item>
        <name>
          <family>Mrevlishvili </family>
          <given>G</given>
        </name>
      </item>
    </creators>
    <title>Collagen photodegradation under UV irradiation </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>The influence of UV irradiation on the collagen triple helix has been studied at the molecular level. It is shown that UV irradiation causes the appearance of primer free radicals in the water surrounding the collagen, which then interact with the proline residue of the protein with the appearance of secondary free radicals. This is connected with destabilization of the collagen molecule as the defects in the amino acid residues probably lead to cleavage of the covalent bonds near the damaged sites, so maintaining the triple helical structure. The presence of ascorbic acid (vitamin C) in the solution protects the collagen molecule from the action of the secondary free radicals. </abstract>
    <date>2005-12</date>
    <date_type>published</date_type>
    <publication>Journal of Biological Physics and Chemistry</publication>
    <volume>5</volume>
    <number>4</number>
    <publisher>AMSI &amp; Collegium Basilea</publisher>
    <pagerange>133-136</pagerange>
    <refereed>TRUE</refereed>
    <issn>1512-0856 </issn>
    <official_url>http://www.amsi.ge/jbpc/</official_url>
  </eprint>
</eprints>
