Work

Polarization Measurements Of Doc-Dependent Ipab-Ipad Interactions

Year: 2017

Type: dataset

Abstract: 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.

Source: Digital Commons - USU (Utah State University)

DOI: 10.5281/zenodo.1042801

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

Institutions: Utah State University, University of Kansas

Language: English

Topic: Escherichia coli research studies

Subfield: Endocrinology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W4393794745

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