Fig. 6: Regions associated with chaperone function are protected during denaturation.

a Ribbon structure of HSP90AA1 (P07901) as predicted by Alphafold v1⁶⁵. Brackets delineated the N-terminal (NTD; responsible for nucleotide binding), middle (MD), and C-terminal (CTD; responsible for dimerization) domains. b Ribbon structure of human T-complex protein Ring Complex (TRiC) derived from PDB 6NRC⁶⁶. Peptides were mapped from Mus musculus to Homo sapiens using blastp alignment. Zoomed and rotated views are also provided for subunits of interest CCT2 (P78371), CCT3 (P49368), CCT6 (P04227) and CCT8 (P50990). Common domain structure comprising the apical domain (substrate binding and lid), intermediate domain, and equatorial domain (ATP-binding) is delineated on CCT2. In all panels, cysteine residues are labeled and colored according to the cluster their respective peptides were assigned (orange, red, purple and blue correspond to clusters 1–4 respectively, black was not observed). Additional residues of interest in substrate binding are colored in green.