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. Author manuscript; available in PMC: 2021 May 23.
Published in final edited form as: Nat Methods. 2020 Nov 23;17(12):1222–1228. doi: 10.1038/s41592-020-00999-z

Extended Data Fig. 8. Examples of relationships between DI-SPA data collection settings for different peptides and their corresponding proteins.

Extended Data Fig. 8

Peptides that uniquely identify proteins are found with a combination of gas-phase fractionation by FAIMS and precursor mass isolation with the first quadrupole (Q1). In this example, two unique peptides from different proteins are co-isolated with FAIMS compensation voltage (CV) of −50 V and Q1 set to 437 m/z. A single peptide is isolated with CV of −70 V and the same Q1 setting of 437 m/z, and two more peptides are isolated with a CV of −80 V at Q1 set to 438.5 m/z. Library spectra are shown for each peptide. The three most abundant singly charged y-ions in the library spectra are used for peptide quantification unless otherwise noted.