Dataset Open Access

Polarization measurements of DOC-dependent IpaB-IpaD interactions

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

Dublin Core Export

<?xml version='1.0' encoding='utf-8'?>
<oai_dc:dc xmlns:dc="" xmlns:oai_dc="" xmlns:xsi="" xsi:schemaLocation="">
  <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: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:title>Polarization measurements of DOC-dependent IpaB-IpaD interactions</dc:title>
All versions This version
Views 255256
Downloads 3434
Data volume 191.8 kB191.8 kB
Unique views 245246
Unique downloads 3333


Cite as