Discover Community Create You

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

Article

Effect of amino acid alterations in the tryptophan-binding site of the trp repressor.

The Journal of biological chemistry - 15 Jan 1990

He J J, Matthews K S

Abstract excerpt

Mutations in the tryptophan-binding site of the trp repressor have been generated using site-directed mutagenesis. The selection of sites for alteration was based on the three-dimensional x-ray crystallographic structure (Schevitz, R. W., Otwinowski, Z., Joachimiak, A., Lawson, C. L., and Sigler, P. B. (1985) Nature 317, 782-786). The changes generated include Thr-44 to Ala (T44A), Arg-54 to Leu (R54L), Arg-54 to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Amino Acids
Share to DNA-Binding Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Molecular Sequence Data

Share to Mutation

Share to Repressor Proteins

Share to Transcription Factors

Source

Identifiers

PMID: 2295616

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of amino acid alterations in the tryptophan-binding site of the trp repressor.PMID 2295616Read ↗

Effects of mutations in the L-tryptophan binding pocket of the Trp RNA-binding attenuation protein of Bacillus subtilis.Semantic proximity Read ↗

Mutant tryptophan aporepressors with altered specificities of corepressor recognition.Semantic proximity Read ↗

An alkaline phosphatase protection assay to investigate trp repressor/operator interactions.Semantic proximity Read ↗

Design and evaluation of a tryptophanless RecA protein with wild type activity.Semantic proximity Read ↗

Spontaneous trpY mutants and mutational analysis of the TrpY archaeal transcription regulator.Semantic proximity Read ↗

The stereochemistry and biochemistry of the trp repressor-operator complex.Semantic proximity Read ↗

Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.Semantic proximity Read ↗

Characterization of charge change super-repressor mutants of trp repressor: effects on oligomerization conformation, ligation and stability.Semantic proximity Read ↗

Enhanced operator binding by trp superrepressors of Escherichia coli.Semantic proximity Read ↗

Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutants.Semantic proximity Read ↗

Analysis of tryptophan residues in the staphylococcal multidrug transporter QacA reveals long-distance functional associations of residues on opposite sides of the membrane.Semantic proximity Read ↗

tRNA(Trp) translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.