A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.

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Article

A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.

The Journal of biological chemistry - 5 Jun 1992

Baneyx F, Gatenby A A

Abstract excerpt

GroEL140, a mutant Escherichia coli chaperonin unable to support bacteriophage lambda head assembly, was purified to near homogeneity and compared to wild type GroEL (cpn60). GroEL140 exhibited a 1.5-fold lower ATPase activity relative to the wild type protein. The hydrolysis of ATP by both polyp...

Topics

Adenine Nucleotides
Adenosine Triphosphatases
Bacterial Proteins
Chaperonin 60
Chromatography, Gel
Escherichia coli
Heat-Shock Proteins
Hydrolysis
Mutation
Plasmids
Protein Conformation
Ribulose-Bisphosphate Carboxylase
Trypsin

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Identifiers

PMID: 1350786

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1350786-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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