November 6, 2017 Dataset Open Access

Bernard, Abram R; Jessop, T. Carson; Kumar, Prashant; Dickenson, Nicholas E.

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  <dc:creator>Bernard, Abram R</dc:creator>
  <dc:creator>Jessop, T. Carson</dc:creator>
  <dc:creator>Kumar, Prashant</dc:creator>
  <dc:creator>Dickenson, Nicholas E.</dc:creator>
  <dc:date>2017-11-06</dc:date>
  <dc:description>The binding affinity between each of the engineered IpaD alanine mutants and the stable IpaB28-226 construct was measured using fluorescence polarization. Here, the DOC effect on binding affinity between IpaB and the engineered IpaD π-helix mutants was quantified by holding IpaB28-226-Alexa568 concentration constant  while the concentration of IpaD or engineered IpaD mutant was titrated from 0-10 μM with identical conditions then tested in the presence of 1 mM DOC.</dc:description>
  <dc:identifier>https://zenodo.org/record/1042802</dc:identifier>
  <dc:identifier>10.5281/zenodo.1042802</dc:identifier>
  <dc:identifier>oai:zenodo.org:1042802</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>doi:10.5281/zenodo.1042801</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>https://creativecommons.org/licenses/by/4.0/legalcode</dc:rights>
  <dc:title>Polarization measurements of DOC-dependent IpaB-IpaD interactions</dc:title>
  <dc:type>info:eu-repo/semantics/other</dc:type>
  <dc:type>dataset</dc:type>
</oai_dc:dc>