<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Chabert, Valentin</dc:creator>
  <dc:creator>Hologne, M.</dc:creator>
  <dc:creator>Sénèque, O.</dc:creator>
  <dc:creator>Crochet, Aurélien</dc:creator>
  <dc:creator>Walker, O.</dc:creator>
  <dc:creator>Fromm, Katharina M.</dc:creator>
  <dc:date>2017-06-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Using model peptides, each of the nine MX2H or HXnM (n = 1, 2) motifs of the silver  resistance protein SilE has been shown to coordinate to one Ag+ ion by its histidine and  methionine residues with Kd in the μM range. This suggests an Ag+ buffering role for SilE  in the case of high Ag+ overload.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/305485</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305485/files/fro_mps.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305485/files/fro_mps_sm.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305485/files/fro_mps_sm2.txt</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1039/C7CC02630G</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Chemical Communications. - 2017, vol. 53, no. 45, p. 6105–6108</dc:source>
  <dc:subject>info:eu-repo/classification/udc/54</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">Model peptide studies of Ag+ binding sites from the silver resistance protein SilE</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>