MassIVE MSV000086748

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Improved Proteoform Characterization using FAIMS in Top-down Proteomic Analysis of Heterogeneous Samples.

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Description

Field Asymmetric Ion Mobility Spectrometry (FAIMS) used in proteomics studies provides superior selectivity and enables more proteins to be identified by providing orthogonal gas phase separation. We sought to test the performance of cylindrical FAIMS in the identification of proteoforms by top-down mass spectrometry of heterogeneous protein mixtures. Combining FAIMS with chromatographic separation resulted in a 60% increase in protein identifications and 18% increase in proteoform identifications as compared to samples analyzed without FAIMS. This increase was attributable, in part, to improved signal-to-noise for proteoforms with similar retention times. Additionally, our results show that the optimal compensation voltage of any given proteoform was correlated with the analytes molecular weight. Collectively these results suggest that FAIMS can enhance top-down proteomics for both discovery and targeted applications. [doi:10.25345/C59J63] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: FAIMS ; Top-down proteomics ; Gas phase separation ; CD3+ T cells

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Principal Investigators:
(in alphabetical order) 		Neil L Kelleher, Northwestern University, United States
Submitting User: rdmelani
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