title: To What Extent is FAIMS Beneficial in the Analysis of Proteins?
abstract: 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.
authors: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. h.j.cooper@bham.ac.uk.
authors: Helen J
authors: HJ
authors: Cooper
mesh_terms: D000818:Animals; D006801:Humans; D007477:Ions / Q000032:analysis; D008099:Liver / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D051379:Mice; D008958:Models, Molecular; D010455:Peptides / Q000032:analysis; D011506:Proteins / Q000032:analysis*; D040901:Proteomics / Q000379:methods; D025801:Ubiquitin / Q000032:analysis
chemical_list: D007477:Ions; D010455:Peptides; D011506:Proteins; D025801:Ubiquitin
keywords: DMS; FAIMS; Peptides; Proteins; Proteomics