Proteomics

Dataset Information

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Folding of beta-tubulin by the chaperonin TRiC/CCT studied by chemical cross-linking and mass spectrometry

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study the folding of the client protein, beta-tubulin, by the chaperonin TRiC/CCT. Different complexes containing TRiC/CCT and/or the chaperone prefoldin were cross-linked in absence or presence of nucleotides with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner  

LAB HEAD: Alexander Leitner

PROVIDER: PXD030590 | Pride | 2022-12-08

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
200804_LU02_aleitner_TRiCtub_02.raw Raw
200804_LU02_aleitner_TRiCtub_04.raw Raw
200804_LU02_aleitner_TRiCtub_06.raw Raw
200804_LU02_aleitner_TRiCtub_09.raw Raw
200804_LU02_aleitner_TRiCtub_11.raw Raw
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