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

Localization of two domains of a mutant form of Escherichia coli protein L7/L12 that binds the large ribosomal subunit as a single dimer.

Biochimie - 1 Jun 1997

Wiggers R J, Hadian H, Traut R R, Oleinikov A V, Glitz D G

Abstract excerpt

Escherichia coli ribosomal protein L7/L12 occurs on the large subunit as two dimers: one dimer is extended and comprises the stalk, while the second dimer is folded and occupies a site on the subunit body. A variant protein, in which all 18 amino acids of the flexible hinge region that links separate N-terminal and C-terminal domains of L7/L12 has been deleted, binds the subunit as a single dimer and does not...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Monoclonal
Share to Bacterial Proteins

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

Share to Binding Sites

Share to Dimerization

Share to Escherichia coli

Share to Mutation

Share to Protein Binding

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 9310186
DOI: 10.1016/s0300-9084(97)80031-4

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

Localization of two domains of a mutant form of Escherichia coli protein L7/L12 that binds the large ribosomal subunit as a single dimer.PMID 9310186Read ↗

Structural and functional domains of Escherichia coli ribosomal protein L7/L12. The hinge region is required for activity.Semantic proximity Read ↗

The proximity of the C-terminal domain of Escherichia coli ribosomal protein L7/L12 to L10 determined by cysteine site-directed mutagenesis and protein-protein cross-linking.Semantic proximity Read ↗

A single-headed dimer of Escherichia coli ribosomal protein L7/L12 supports protein synthesis.Semantic proximity Read ↗

Location and domain structure of Escherichia coli ribosomal protein L7/L12: site specific cysteine crosslinking and attachment of fluorescent probes.Semantic proximity Read ↗

Dimer/monomer equilibrium and domain separations of Escherichia coli ribosomal protein L7/L12.Semantic proximity Read ↗

Tetramethylrhodamine dimer formation as a spectroscopic probe of the conformation of Escherichia coli ribosomal protein L7/L12 dimers.Semantic proximity Read ↗

Delta Lys120, a mutation which destabilizes the ribosome-binding domain of ribosomal protein L7/L12.Semantic proximity Read ↗

Mapping the essential structures of human ribosomal protein L7 for nuclear entry, ribosome assembly and function.Semantic proximity Read ↗

Structure function relationships in the ribosomal stalk proteins of archaebacteria.Semantic proximity Read ↗

Study of tyrosine-containing mutants of ribosomal protein L7/L12 from Escherichia coli.Semantic proximity Read ↗

Dimerisation mutants of Lac repressor. II. A single amino acid substitution, D278L, changes the specificity of dimerisation.Semantic proximity Read ↗

Structural analysis of interdomain mobility in ribosomal L1 proteins.Semantic proximity Read ↗

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