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Article

A fluorescence study of Tn10-encoded tet repressor.

Journal of protein chemistry - 1 Jan 1996

Wasylewski Z, Kaszycki P, Drwiega M

Abstract excerpt

Steady-state fluorescence quenching and time-resolved measurements have been performed to resolve the fluorescence contributions of the two tryptophan residues, W43 and W75, in the subunit of the homodimer of the Tet repressor from Escherichia coli. The W43 residue is localized within the helix-t...

Topics

Acrylamide
Acrylamides
Bacterial Proteins
DNA Nucleotidyltransferases
Escherichia coli
Fluorescence
Helix-Turn-Helix Motifs
Molecular Conformation
Mutation
Potassium Iodide
Repressor Proteins
Spectrometry, Fluorescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Succinimides

Temperature

Transposases

Tryptophan

Source

Identifiers

PMID: 8838589
DOI: 10.1007/BF01886810

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8838589-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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A fluorescence study of Tn10-encoded tet repressor.PMID 8838589Read ↗

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