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. Author manuscript; available in PMC: 2023 Feb 22.
Published in final edited form as: Anal Chem. 2022 Feb 10;94(7):3328–3334. doi: 10.1021/acs.analchem.1c05398

Figure 1. Overview of peptide identification and TMT quantitation with MultiNotch IRMPD MS3.

Figure 1.

a) Stable isobaric labeling of peptides allows for quantitative mass spectrometry-based proteomics experiments in which differentially tagged peptides appear indistinguishable in MS1 scans. b) Fragmentation by lower energy HCD produces sequence informative b- and y-type ions and limited reporter ions. c) MultiNotch Synchronous Precursor Selection allows for isolation and fragmentation of high signal fragment ions by either higher energy HCD or IRMPD. d) A MS1 survey scan reveals precursor targets for e) data dependent MS2 acquisition with lower energy HCD. f) Synchronous selection of the top ten most abundant fragment ions allows for either higher energy or IRMPD to increase reporter ion generation.