Extended Data Fig. 5: HDX-MS of Ancα/β.
a–c, Deuterium uptake measurements across time for three peptides. Left vertical axis, raw deuterium incorporation; right vertical axis, deuterium incorporation divided by the total number of exchangeable amide hydrogens per peptide. Uptake curves for four concentrations of mutants IF1rev and P127R are shown. Each point shows mean ± s.e. of three replicate measurements. d–f, Raw MS spectra for the peptides shown in a–c, respectively, at 0.67 μM (red, at which the protein is monomeric), and 75 μM (purple, at which it is entirely dimeric: see Extended Data Fig. 2). The traces are slightly offset to allow visualization. One replicate at each incubation time is shown. g, Amino acids 99 to 111 contact IF1 (orange) or IF2 (yellow). The homology model of one chain of Ancα/β (cartoon and sticks) was aligned to the α-subunit of human Hb (PDB 1A3N); β-subunits are shown as surfaces. h, Normalized deuterium uptake difference (mean ± s.e. from three replicates), defined as the uptake difference between monomer and dimer divided by the uptake of the monomer, observed for peptides containing amino acids 99–111. Grey N-terminal residues do not contribute to uptake. Amino acid sequences are aligned and labelled (orange dots, IF1; yellow dots, IF2).
