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Article

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

The Journal of biological chemistry - 6 Aug 1999

Aramli L A, Teschke C M

Abstract excerpt

The amino acid sequence of a polypeptide defines both the folding pathway and the final three-dimensional structure of a protein. Eighteen amino acid substitutions have been identified in bacteriophage P22 coat protein that are defective in folding and cause their folding intermediates to be substrates for GroEL and GroES. These temperature-sensitive folding (tsf) substitutions identify amino acids that are...

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Share to Bacteriophage P22
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10428787
DOI: 10.1074/jbc.274.32.22217

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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.

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Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.PMID 10428787Read ↗

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

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

Isolation of suppressors of temperature-sensitive folding mutations.Semantic proximity Read ↗

GroEL binds a late folding intermediate of phage P22 coat protein.Semantic proximity Read ↗

The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype.Semantic proximity Read ↗

A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Semantic proximity Read ↗

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

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

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

Alleviation of a defect in protein folding by increasing the rate of subunit assembly.Semantic proximity Read ↗

In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivity.Semantic proximity Read ↗

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

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