Proteomics

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In situ observation of chaperonin function in protein folding


ABSTRACT: 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 used cryo-electron tomography in situ to visualize and quantify functional GroEL:ES complexes in their intact cellular environment. Mass spectrometry was used to estimate stoichiometries of GroEL, GroES, cellular ribosome content and substrates.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Roman Körner  

LAB HEAD: F. Ulrich Hartl

PROVIDER: PXD042587 | Pride | 2024-06-27

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20200616_HF_JW_20493.raw Raw
20200616_HF_JW_20494.raw Raw
20200616_HF_JW_20495.raw Raw
20200616_HF_JW_20496.raw Raw
20200616_HF_JW_20497.raw Raw
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