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ProteomicsDnaK interaction and folding of firefly luciferase studied by hydrogen/deuterium exchange – mass spectrometry
The ATP-dependent chaperones of the Hsp70 class (DnaK in E. coli) function in protein folding in cooperation with J proteins and nucleotide exchange factors (DnaJ and GrpE in E. coli, respectively). Hsp70 prevents protein aggregation, increasing the folding yield, but whether it also enhances the ra...
ORGANISM(S): Escherichia coli 
2020-01-15 | PXD016509 | Pride
Deuterium exchange Chaperone Firefly luciferase Dnak Folding 
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 
ProteomicsAnalysis of stalled ribosome-nascent chain complexes by quantitative proteomics
The cellular environment is critical for efficient protein maturation, but how proteins fold during biogenesis remains poorly understood. To understand how the cellular environment modulates folding, we studied the cotranslational chaperone-assisted folding of Escherichia coli dihydrofolate reductas...
ORGANISM(S): Escherichia coli 
2025-05-06 | PXD036784 | Pride
Protein biosynthesis Ribosome-nascent chain complexes Interactome Protein folding Lc-ms/ms 
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