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

DNA binding and oligomerization of NtrC studied by fluorescence anisotropy and fluorescence correlation spectroscopy.

Nucleic acids research - 15 Mar 1998

Sevenich F W, Langowski J, Weiss V, Rippe K

Abstract excerpt

Fluorescence anisotropy and fluorescence correlation spectroscopy measurements of rhodamine-labeled DNA oligonucleotide duplexes have been used to determine equilibrium binding constants for DNA binding of the prokaryotic transcription activator protein NtrC. Measurements were made with wild-type NtrC from Escherichia coli and the constitutively active mutant NtrCS160Ffrom Salmonella using DNA duplexes with one...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Amino Acid Sequence
Share to Base Sequence

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

Share to DNA-Binding Proteins

Share to Escherichia coli

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 9490780
DOI: 10.1093/nar/26.6.1373
PMCID: PMC147426

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

DNA binding and oligomerization of NtrC studied by fluorescence anisotropy and fluorescence correlation spectroscopy.PMID 9490780Read ↗

Properties of a mutant form of the prokaryotic enhancer binding protein, NTRC, which hydrolyses ATP in the absence of effectors.Semantic proximity Read ↗

The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain.Semantic proximity Read ↗

Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain.Semantic proximity Read ↗

Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: a third function for the C-terminal domain.Semantic proximity Read ↗

Quantitative analysis of the ternary complex of RNA polymerase, cyclic AMP receptor protein and DNA by fluorescence anisotropy measurements.Semantic proximity Read ↗

The function of isolated domains and chimaeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae.Semantic proximity Read ↗

Detection of tetramerization domains in vivo by cooperative DNA binding to tandem lambda operator sites.Semantic proximity Read ↗

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

Purification and in vitro activities of the Bacillus subtilis TnrA transcription factor.Semantic proximity Read ↗

Influence of a mutation in the putative nucleotide binding site of the nitrogen regulatory protein NTRC on its positive control function.Semantic proximity Read ↗

Probing the physical basis for trp repressor-operator recognition.Semantic proximity Read ↗

Domains formed within the N-terminal region of the quorum-sensing activator TraR are required for transcriptional activation and direct interaction with RpoA from agrobacterium.Semantic proximity Read ↗

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