NDLI: To What Extent is FAIMS Beneficial in the Analysis of Proteins?

Content Provider	Springer Nature Link
Author	Cooper, Helen J.
Copyright Year	2016
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. Graphical Abstract ᅟ
Starting Page	566
Ending Page	577
Page Count	12
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	27
Issue Number	4
e-ISSN	18791123
Language	English
Publisher	Springer US
Publisher Date	2016-02-02
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	FAIMS DMS Proteins Proteomics Peptides Analytical Chemistry Biotechnology Organic Chemistry Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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To What Extent is FAIMS Beneficial in the Analysis of Proteins?