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Article

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.

Cell - 9 Feb 1996

Weissman J S, Rye H S, Fenton W A, Beechem J M, Horwich A L

Abstract excerpt

Recent studies of GroE-mediated protein folding indicate that substrate proteins are productively released from a cis ternary complex in which the nonnative substrate is sequestered within the GroEL channel underneath GroES. Here, we examine whether protein folding can occur in this space. Stopped-flow fluorescence anisotropy of a pyrene-rhodanese-GroEl complex indicates that addition of GroES and ATP (but not...

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Identifiers

PMID: 8608602
DOI: 10.1016/s0092-8674(00)81293-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.PMID 8608602Read ↗

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

Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE.Semantic proximity Read ↗

GroEL Ring Separation and Exchange in the Chaperonin Reaction.Semantic proximity Read ↗

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.Semantic proximity Read ↗

Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.Semantic proximity Read ↗

A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES.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 ↗

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.Semantic proximity Read ↗

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

Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.Semantic proximity Read ↗

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.Semantic proximity Read ↗

Coupling between protein folding and allostery in the GroE chaperonin system.Semantic proximity Read ↗

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