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

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

Scientific reports - 22 Jun 2016

Moparthi Satish Babu, Carlsson Uno, Vincentelli Renaud, Jonsson Bengt-Harald, Hammarström Per, Wenger Jérôme

Abstract excerpt

Here, we study and compare the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from E. coli. MreB is a homologue to actin in prokaryotes. Single-molecule fluorescence correlation spectroscopy (FCS) and time-resolved fluorescence polarization anisotropy report the binding interaction of folding MreB with GroEL, GroES and TRiC. Fluorescence resonance...

Read the complete abstract on PubMed

Topics

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

Share to Actins
Share to Chaperonin 10

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chaperonin 60

Share to Escherichia coli Proteins

Share to Fluorescence Resonance Energy Transfer

Share to Protein Conformation

Share to Protein Folding

Share to Single Molecule Imaging

Source

Open in PubMed Open full text

Identifiers

PMID: 27328749
DOI: 10.1038/srep28386
PMCID: PMC4916439

Genes

PNP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.PMID 27328749Read ↗

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

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

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.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 ↗

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

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

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

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

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

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

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Semantic proximity Read ↗

Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.Semantic proximity Read ↗

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