Polarization measurements of DOC-dependent IpaB-IpaD interactions
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.
Mechanisms of Type III Secretion System ATPase Activation and Regulation
Deoxycholate-Enhanced Shigella Virulence Is Regulated by a Rare π-Helix in the Type Three Secretion System Tip Protein IpaD Abram R. Bernard, T. Carson Jessop, Prashant Kumar, and Nicholas E. Dickenson Biochemistry 2017 56 (49), 6503-6514 DOI: 10.1021/acs.biochem.7b00836
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Bernard, Abram R.; Jessop, Terry; Kumar, Prashant; and Dickenson, Nicholas E., "Polarization measurements of DOC-dependent IpaB-IpaD interactions" (2017). Browse all Datasets. Paper 38.