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ProteomicsGroEL interaction and folding of MetF studied by hydrogen/deuterium exchange – mass spectrometry
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in E. coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and the lid-shaped GroES. We analyzed the spontaneous and chaperonin-assisted folding of the essen...
ORGANISM(S): Escherichia coli 
2020-03-05 | PXD016666 | Pride
Groel Chaperone Folding Metf Hydrogen/deuterium exchange Chaperonin 
UnknownProtein chain collapse modulation and folding stimulation by GroEL-ES.
Not available
S-EPMC8896798 | biostudies-literature
UnknownGroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.
Not available
S-EPMC4071350 | biostudies-literature
UnknownVisualizing GroEL/ES in the act of encapsulating a folding protein.
Not available
S-EPMC3695626 | biostudies-literature
UnknownDifferential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.
Not available
S-EPMC4916439 | biostudies-literature
UnknownGroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.
Not available
S-EPMC12615815 | biostudies-literature
ProteomicsIn situ observation of chaperonin function in protein folding
The GroEL/GroES chaperonin mediates protein folding in bacteria in an ATP-dependent process. Studies in vitro show that the GroEL double-ring and the lid-shaped GroES transiently encapsulate unfolded protein for folding unimpaired by aggregation. To clarify critical aspects of this mechanism, we use...
ORGANISM(S): Escherichia coli 
2024-06-27 | PXD042587 | Pride
Chaperonin Atpase Chaperone Heat shock Folding cage Proteostasis 
ProteomicsCotranslational activity of the GroEL chaperonin
Various proteins in the cell begin to fold during synthesis at the ribosome, many with the assistance of molecular chaperones. While the cotranslational activity of ribosome-associated chaperones and Hsp70 is frequently studied, the role of Hsp60 chaperonins during protein synthesis remains poorly u...
ORGANISM(S): Escherichia coli 
2025-10-14 | PXD054376 | Pride
Groel Hdx-ms Rnc 
UnknownA diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.
Not available
S-EPMC9860310 | biostudies-literature
UnknownHydroxybiphenylamide GroEL/ES Inhibitors Are Potent Antibacterials against Planktonic and Biofilm Forms of Staphylococcus aureus.
Not available
S-EPMC6467803 | biostudies-literature
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