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Article

Coupling between protein folding and allostery in the GroE chaperonin system.

Proceedings of the National Academy of Sciences of the United States of America - 15 Feb 2000

Yifrach O, Horovitz A

Abstract excerpt

GroEL is an allosteric protein that facilitates protein folding in an ATP-dependent manner. Herein, the relationship between cooperative ATP binding by GroEL and the kinetics of GroE-assisted folding of two substrates with different GroES dependence, mouse dihydrofolate reductase (mDHFR) and mitochondrial malate dehydrogenase, is examined by using cooperativity mutants of GroEL. Strong intra-ring positive...

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

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Source

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Identifiers

PMID: 10677493
DOI: 10.1073/pnas.040449997
PMCID: PMC26467

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Coupling between protein folding and allostery in the GroE chaperonin system.PMID 10677493Read ↗

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Triggering protein folding within the GroEL-GroES complex.Semantic proximity Read ↗

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.Semantic proximity Read ↗

Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.Semantic proximity Read ↗

Kinetic analysis of ATP-dependent inter-ring communication in GroEL.Semantic proximity Read ↗

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Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Semantic proximity Read ↗

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