Fig. 1.

Mass spectrometric dissociation of the RA33 epitope peptide – antiRA33 antibody complex and amino acid sequence determination of the complex-released peptide by mass spectrometric fragmentation. Ion mobility arrival time plots of A, Solution 1, C, and E, Solution 3. Dashed lines mark the regions for mass spectra selections. Settings of the TRAP cell, the TRANSFER cell, and the quadrupole are indicated at the right. B, D, and F, nanoESI mass spectra (low m/z range) of ions from selected arrival time ranges. Selected m/z values are given and charge states are indicated in parentheses. For ion signal assignments see supplemental Table S1. G, Amino acid sequence of the complex-released peptide (single letter code) as determined by the matched mass spectrometric fragment ions (fragment ion types and numbers are indicated). The Uniprot protein ID of the peptide source protein (first hit) is shown. H, Pseudo mass spectrum (after charge deconvolution and de-isotoping) of fragment ions derived by selecting arrival time of the complex-released peptide with m/z 817.48. For ion signal assignments see supplemental Table S2.