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UnknownCotranslational folding increases GFP folding yield.
Not available
S-EPMC2849091 | biostudies-literature
TranscriptomicsSelective ribosome profiling reveals the co-translational chaperone action of trigger factor in vivo
As nascent polypeptides exit ribosomes, they are engaged by a series of processing, targeting and folding factors. Here we present a selective ribosome profiling strategy that enables global monitoring of when these factors engage polypeptides in the complex cellular environment. Studies of the Esch...
ORGANISM(S): Escherichia coli 
2011-12-09 | E-GEOD-33671 | biostudies-arrayexpress
UnknownPathway regulation mechanism by cotranslational protein folding.
Not available
S-EPMC12316862 | biostudies-literature
ProteomicsMechanism of chaperone coordination during cotranslational protein folding in bacteria
Protein folding is assisted by molecular chaperones that bind nascent polypeptides during mRNA translation. Several structurally-distinct classes of chaperone promote de novo folding, suggesting that their activities are coordinated at the ribosome. We used biochemical reconstitution and structural ...
ORGANISM(S): Escherichia coli 
2024-07-03 | PXD048623 | Pride
Nascent chain Ribosomes Xl-ms Molecular chaperones Protein synthesis Β-galactosidase Protein folding 
ProteomicsMechanism of chaperone coordination during cotranslational protein folding in bacteria
Protein folding is assisted by molecular chaperones that bind nascent polypeptides during mRNA translation. Several structurally-distinct classes of chaperones promote de novo folding, suggesting that their activity is coordinated at the ribosome. Here we use biochemical reconstitution and structura...
ORGANISM(S): Escherichia coli 
2024-07-03 | PXD048645 | Pride
Nascent chain Ribosomes Ms Molecular chaperones Protein synthesis Β-galactosidase Protein folding 
UnknownEvidence of evolutionary selection for cotranslational folding.
Not available
S-EPMC5664504 | biostudies-literature
ProteomicsMechanism of chaperone coordination during cotranslational protein folding in bacteria
Protein folding is assisted by molecular chaperones that bind nascent polypeptides during mRNA translation. Several structurally-distinct classes of chaperones promote de novo folding, suggesting that their activity is coordinated at the ribosome. Here we use biochemical reconstitution and structura...
ORGANISM(S): Escherichia coli 
2024-07-03 | PXD048642 | Pride
Nascent chain Ribosomes Hdx-ms Molecular chaperones Protein synthesis Β-galactosidase Protein folding 
ProteomicsMechanism of chaperone coordination during cotranslational protein folding in bacteria
Protein folding is assisted by molecular chaperones that bind nascent polypeptides during mRNA translation. Several structurally-distinct classes of chaperones promote de novo folding, suggesting that their activity is coordinated at the ribosome. Here we use biochemical reconstitution and structura...
ORGANISM(S): Escherichia coli 
2024-07-03 | PXD048638 | Pride
Nascent chain Ribosomes Hdx-ms Molecular chaperones Protein synthesis Β-galactosidase Protein folding 
UnknownCotranslational protein folding through non-native structural intermediates.
Not available
S-EPMC12412654 | biostudies-literature
UnknownEffect of Protein Structure on Evolution of Cotranslational Folding.
Not available
S-EPMC7499064 | biostudies-literature
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