Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Proteins - 1 Oct 2012

Skjaerven Lars, Muga Arturo, Reuter Nathalie, Martinez Aurora

Abstract excerpt

The molecular chaperone, GroEL, essential for correct protein folding in E. coli, is composed of 14 identical subunits organized in two interacting rings, each providing a folding chamber for non-native substrate proteins. The oligomeric assembly shows positive cooperativity within each ring and negative cooperativity between the rings. Although it is well known that ATP and long-range allosteric interactions...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Chaperonin 10
Share to Chaperonin 60

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Molecular Dynamics Simulation

Share to Principal Component Analysis

Share to Protein Conformation

Source

Identifiers

PMID: 22576372
DOI: 10.1002/prot.24113

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES.PMID 22576372Read ↗

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

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

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

Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations.Semantic proximity Read ↗

Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.Semantic proximity Read ↗

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

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

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.Semantic proximity Read ↗

A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.Semantic proximity Read ↗

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

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

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.