Multiplexed mass spectrometry of individual ions improves measurement of proteoforms and their complexes

Jared O. Kafader, Rafael D. Melani, Kenneth R. Durbin, Bon Ikwuagwu, Bryan P. Early, Ryan T. Fellers, Steven C. Beu, Vlad Zabrouskov, Alexander A. Makarov, Joshua T. Maze, Deven L. Shinholt, Ping F. Yip, Danielle Tullman-Ercek, Michael W. Senko, Philip D. Compton*, Neil L. Kelleher

*Corresponding author for this work

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

An Orbitrap-based ion analysis procedure determines the direct charge for numerous individual protein ions to generate true mass spectra. This individual ion mass spectrometry (I2MS) method for charge detection enables the characterization of highly complicated mixtures of proteoforms and their complexes in both denatured and native modes of operation, revealing information not obtainable by typical measurements of ensembles of ions.

Original languageEnglish (US)
Pages (from-to)391-394
Number of pages4
JournalNature Methods
Volume17
Issue number4
DOIs
StatePublished - Apr 1 2020

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Kafader, J. O., Melani, R. D., Durbin, K. R., Ikwuagwu, B., Early, B. P., Fellers, R. T., Beu, S. C., Zabrouskov, V., Makarov, A. A., Maze, J. T., Shinholt, D. L., Yip, P. F., Tullman-Ercek, D., Senko, M. W., Compton, P. D., & Kelleher, N. L. (2020). Multiplexed mass spectrometry of individual ions improves measurement of proteoforms and their complexes. Nature Methods, 17(4), 391-394. https://doi.org/10.1038/s41592-020-0764-5