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The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52. Because of the many proteins involved in these interactions it is often difficult to delineate all possible combinations of subunits in the complexes formed. We employed mass spectrometry to monitor the assembly and to determine the favoured pathways within these chaperone cycles. Combining the subunit composition with chemical cross-linking and proteomics allowed us to define interaction interfaces, protein dynamics and new intermediates.

Original publication




Journal article



Publication Date





18276 - 18281


Hsp70/90 chaperone cycle, client proteins, co-chaperones, cross-linking, mass spectrometry, Animals, Binding Sites, HSP40 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Homeodomain Proteins, Humans, Mass Spectrometry, Models, Molecular, Molecular Chaperones, Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Recombinant Proteins, Sf9 Cells, Tacrolimus Binding Proteins, Tumor Suppressor Proteins