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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-turn-helix structural domain, which is responsible for sequence-specific binding of the Tet repressor to the tet...

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Identifiers

PMID: 8838589
DOI: 10.1007/BF01886810

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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

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Fluorescence quenching studies of Trp repressor using single-tryptophan mutants.Semantic proximity Read ↗

Quantitative analysis of Tn10 Tet repressor binding to a complete set of tet operator mutants.Semantic proximity Read ↗

A peptide triggers allostery in tet repressor by binding to a unique site.Semantic proximity Read ↗

Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.Semantic proximity Read ↗

Luminescence studies with trp repressor and its single-tryptophan mutants.Semantic proximity Read ↗

Conformational dynamics of the tetracycline-binding aptamer.Semantic proximity Read ↗

A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data.Semantic proximity Read ↗

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Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb.Semantic proximity Read ↗

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