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

Intragenic suppressors of folding defects in the P22 tailspike protein.

Genetics - 1 Feb 1991

Fane B, King J

Abstract excerpt

Within the amino acid sequences of polypeptide chains little is known of the distribution of sites and sequences critical for directing chain folding and assembly. Temperature-sensitive folding (tsf) mutations identifying such sites have been previously isolated and characterized in gene 9 of phage P22 encoding the tailspike endorhamnosidase. We report here the isolation of a set of second-site conformational...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Chromosome Mapping
Share to Crosses, Genetic

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

Share to Genetic Complementation Test

Share to Kinetics

Share to Mutation

Share to Phenotype

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 1825987
DOI: 10.1093/genetics/127.2.263
PMCID: PMC1204354

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

Intragenic suppressors of folding defects in the P22 tailspike protein.PMID 1825987Read ↗

Isolation of suppressors of temperature-sensitive folding mutations.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 ↗

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

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

Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Semantic proximity Read ↗

A tail of protein folding.Semantic proximity Read ↗

Intragenic suppression of a capsid assembly-defective P22 tailspike mutation.Semantic proximity Read ↗

Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.Semantic proximity Read ↗

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