Amide hydrogen exchange and internal dynamics in the chemotactic protein CheY from Escherichia coli.

doi:10.1006/jmbi.1997.1178

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Article

Amide hydrogen exchange and internal dynamics in the chemotactic protein CheY from Escherichia coli.

Journal of molecular biology - 22 Aug 1997

Lacroix E, Bruix M, López-Hernández E, Serrano L, Rico M

Abstract excerpt

The backbone internal dynamics of the wild-type 129 amino acid alpha/beta parallel protein CheY and its double mutant F14N/P110G are analysed here by the hydrogen-exchange method. The F14N mutation is known to stabilise the protein and to accelerate refolding while P110G is destabilising and acce...

Topics

Amides
Amino Acid Sequence
Bacterial Proteins
Chemotaxis
Escherichia coli
Escherichia coli Proteins
Hydrogen
Magnetic Resonance Spectroscopy
Membrane Proteins
Methyl-Accepting Chemotaxis Proteins
Molecular Sequence Data
Mutation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary

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Identifiers

PMID: 9268672
DOI: 10.1006/jmbi.1997.1178

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9268672-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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