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

Study of tyrosine-containing mutants of ribosomal protein L7/L12 from Escherichia coli.

Biophysical chemistry - 29 Nov 1996

Todorova R T, Rogov V V, Vasilenko K S, Permyakov E A

Abstract excerpt

Three mutant forms of the ribosomal protein L7/L12 with replacements of Ser1, Met14 and Met26 to Tyr were studied by the methods of fluorescence spectroscopy, circular dichroism and microcalorimetry. The amino-acid residue Tyr14 in the protein L7/L12 Tyr14 is located in a region with a more organized structure than Tyr26 in protein L7/L12 Tyr26. The replacements Ser1-->Tyr1 and Met14-->Tyr14 do not affect the...

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 Circular Dichroism
Share to Escherichia coli

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

Share to Hydrogen-Ion Concentration

Share to Mutation

Share to Protein Denaturation

Share to Temperature

Share to Tyrosine

Source

Identifiers

PMID: 8962470
DOI: 10.1016/s0301-4622(96)02176-x

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

Study of tyrosine-containing mutants of ribosomal protein L7/L12 from Escherichia coli.PMID 8962470Read ↗

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

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

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 ↗

Role of the ribosomal protein L27 revealed by single-molecule FRET study.Semantic proximity Read ↗

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

Changes in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation analysis.Semantic proximity Read ↗

[Crystal structures of mutant ribosomal proteins L1].Semantic proximity Read ↗

Control of phosphate release from elongation factor G by ribosomal protein L7/12.Semantic proximity Read ↗

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

NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of the native conformation of peripheral loops for activity.Semantic proximity Read ↗

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

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