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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): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Leitner

LAB HEAD: Alexander Leitner

PROVIDER: PXD030590 | Pride | 2022-12-08

REPOSITORIES: Pride

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			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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