To what extent is FAIMS beneficial in the analysis of proteins?

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High field asymmetric waveform ion mobility spectrometry (FAIMS), also known as differential ion mobility spectrometry, is emerging as a tool for biomolecular analysis. In this article, the benefits and limitations of FAIMS for protein analysis are discussed. The principles and mechanisms of FAIMS separation of ions are described, and the differences between FAIMS and conventional ion mobility spectrometry are detailed. Protein analysis is considered from both the top-down (intact proteins) and the bottom-up (proteolytic peptides) perspective. The roles of FAIMS in the analysis of complex mixtures of multiple intact proteins and in the analysis of multiple conformers of a single protein are assessed. Similarly, the application of FAIMS in proteomics and targeted analysis of peptides are considered. Graphical Abstract ᅟ.

Original languageEnglish
Pages (from-to)566-577
JournalJournal of the American Society for Mass Spectrometry
Issue number4
Early online date2 Feb 2016
Publication statusPublished - Apr 2016


  • DMS
  • Proteins
  • Proteomics
  • Peptides


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