Polarization measurements of DOC-dependent IpaB-IpaD interactions

Creators

Abram R. Bernard, Utah State UniversityFollow
Terry JessopFollow
Prashant Kumar, University of KansasFollow
Nicholas E. Dickenson, Utah State UniversityFollow

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.

OCLC

1078404618

Document Type

Dataset

DCMI Type

Dataset

File Format

.csv

Publication Date

11-6-2017

Funder

NIH

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

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

Recommended Citation

Bernard, A. R., Jessop, T. C., Kumar, P., & Dickenson, N. E. (2017). Polarization Measurements Of Doc-Dependent Ipab-Ipad Interactions. Zenodo. https://doi.org/10.5281/ZENODO.1042802