Published November 6, 2017
| Version v1
Dataset
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Polarization measurements of DOC-dependent IpaB-IpaD interactions
Authors/Creators
- 1. Department of Chemistry and Biochemistry, Utah State University
- 2. Department of Pharmaceutical Chemistry, University of Kansas,
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.
Files
IpaB IpaD polarization data.csv
Files
(5.6 kB)
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