In vivo activities of GroEL minichaperones.

doi:10.1073/pnas.95.17.9861

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Article

In vivo activities of GroEL minichaperones.

Proceedings of the National Academy of Sciences of the United States of America - 18 Aug 1998

Chatellier J, Hill F, Lund P A, Fersht A R

Abstract excerpt

Fragments encompassing the apical domain of GroEL, called minichaperones, facilitate the refolding of several proteins in vitro without requiring GroES, ATP, or the cage-like structure of multimeric GroEL. We have identified the smallest minichaperone that is active in vitro in chaperoning the re...

Topics

Alleles
Bacteriophage lambda
Base Sequence
Chaperonin 60
DNA Primers
Escherichia coli
Genetic Complementation Test
Models, Molecular
Mutagenesis, Site-Directed
Peptide Fragments
Protein Conformation
Protein Folding
Recombinant Proteins
Replication Origin
Temperature
Virus Replication

Source

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Identifiers

PMID: 9707566
DOI: 10.1073/pnas.95.17.9861
PMCID: PMC21427

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9707566-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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