<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, Maggy</dc:creator>
  <dc:creator>Sénèque, Olivier</dc:creator>
  <dc:creator>Walker, Olivier</dc:creator>
  <dc:creator>Fromm, Katharina M.</dc:creator>
  <dc:date>2018-09-13</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The SilE protein is suspected to have a prominent role in Ag+ detoxification of silver  resistant bacteria. Using model peptides, we elucidated both qualitative and quantitative  aspects of the Ag+-induced α-helical structuring role of His- and Met-rich sequences of  SilE, improving our understanding of its function within the Sil system.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/307335</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307335/files/fro_ahf.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307335/files/fro_ahf_sm.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1039/C8CC03784A</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Chemical Communications. - 2018, vol. 54, no. 74, p. 10419–10422</dc:source>
  <dc:subject>info:eu-repo/classification/udc/54</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">Alpha-helical folding of SilE models upon Ag(His)(Met) motif formation</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>