Title

Polarization measurements of DOC-dependent IpaB-IpaD interactions

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.

Document Type

Dataset

DCMI Type

Dataset

File Format

.csv

Publication Date

11-6-2017

Publisher

Zenodo

Award Number

NIH 1R15AI124108-01A1

Award Title

Mechanisms of Type III Secretion System ATPase Activation and Regulation

Referenced by

Bernard, A. R., Jessop, T. C., Kumar, P., & Dickenson, N. E. (2017). Deoxycholate-Enhanced Shigella Virulence Is Regulated by a Rare π-Helix in the Type Three Secretion System Tip Protein IpaD. Biochemistry, 56(49), 6503–6514. https://doi.org/10.1021/acs.biochem.7b00836

Language

eng

License

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

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