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Article

Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutants.

Biophysical journal - 1 Aug 1990

Royer C A, Gardner J A, Beechem J M, Brochon J C, Matthews K S

Abstract excerpt

We have studied the time-resolved intrinsic tryptophan fluorescence of the lac repressor (a symmetric tetramer containing two tryptophan residues per monomer) and two single-tryptophan mutant repressors obtained by site-directed mutagenesis, lac W201Y and lac W220Y. These mutant repressor proteins have tyrosine substituted for tryptophan at positions 201 and 220, respectively, leaving a single tryptophan residue...

Topics

Ligands
Macromolecular Substances
Mutation
Protein Conformation
Repressor Proteins
Spectrometry, Fluorescence
Tryptophan

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2207244
DOI: 10.1016/S0006-3495(90)82383-3
PMCID: PMC1280978

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2207244-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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