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

Isolation of suppressors of temperature-sensitive folding mutations.

Journal of bacteriology - 1 Jan 1994

Villafane R, Fleming A, Haase-Pettingell C

Abstract excerpt

Mutations in the tailspike gene (gene 9) of Salmonella typhimurium phage P22 have been used to identify amino acid interactions during the folding of a polypeptide chain. Since temperature-sensitive folding (tsf) mutations cause folding defects in the P22 tailspike polypeptide chain, it is likely that mutants derived from these and correcting the original tsf defects (second-site intragenic suppressors) identify...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Electrophoresis, Polyacrylamide Gel
Share to Genes, Viral

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

Share to Molecular Sequence Data

Share to Mutation

Share to Salmonella typhimurium

Share to Sequence Analysis, DNA

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 8282689
DOI: 10.1128/jb.176.1.137-142.1994
PMCID: PMC205024

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

Isolation of suppressors of temperature-sensitive folding mutations.PMID 8282689Read ↗

Intragenic suppressors of folding defects in the P22 tailspike protein.Semantic proximity Read ↗

Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein.Semantic proximity Read ↗

Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase.Semantic proximity Read ↗

Suppressor mutations derived from the most severe protein folding mutation known.Semantic proximity Read ↗

Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.Semantic proximity Read ↗

Side-chain specificity at three temperature-sensitive folding mutation sites of P22 tailspike protein.Semantic proximity Read ↗

Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22.Semantic proximity Read ↗

A tail of protein folding.Semantic proximity Read ↗

P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain.Semantic proximity Read ↗

Global suppression of protein folding defects and inclusion body formation.Semantic proximity Read ↗

Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.Semantic proximity Read ↗

Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype.Semantic proximity Read ↗

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