Fluorescence Measurement of Kinetics of CheY Autophosphorylation with Small Molecule Phosphodonors.

doi:10.1007/978-1-4939-7577-8_25

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Fluorescence Measurement of Kinetics of CheY Autophosphorylation with Small Molecule Phosphodonors.

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2018

Silversmith Ruth E, Bourret Robert B

Abstract excerpt

The Escherichia coli chemotaxis protein CheY is a model receiver domain containing a native tryptophan residue that serves as a fluorescent probe for CheY autophosphorylation with small molecule phosphodonors. Here we describe fluorescence measurement of apparent bimolecular rate constants for reaction of wild type and mutant CheY with phosphodonors acetyl phosphate, phosphoramidate, or monophosphoimidazole....

Topics

Amides
Chemotaxis
Escherichia coli
Escherichia coli Proteins
Imidazoles
Kinetics
Methyl-Accepting Chemotaxis Proteins
Mutation
Organophosphates
Phosphoric Acids
Phosphorylation
Small Molecule Libraries
Spectrometry, Fluorescence

Source

Open in PubMed

Identifiers

PMID: 29429101
DOI: 10.1007/978-1-4939-7577-8_25

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics