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

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 s...

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Autor principal: Cooper, Helen J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4792363/
https://www.ncbi.nlm.nih.gov/pubmed/26843211
http://dx.doi.org/10.1007/s13361-015-1326-4
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author Cooper, Helen J.
author_facet Cooper, Helen J.
author_sort Cooper, Helen J.
collection PubMed
description 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. [Figure: see text]
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spelling pubmed-47923632016-04-09 To What Extent is FAIMS Beneficial in the Analysis of Proteins? Cooper, Helen J. J Am Soc Mass Spectrom Critical Insight 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. [Figure: see text] Springer US 2016-02-02 2016 /pmc/articles/PMC4792363/ /pubmed/26843211 http://dx.doi.org/10.1007/s13361-015-1326-4 Text en © The Author(s) 2016 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Critical Insight
Cooper, Helen J.
To What Extent is FAIMS Beneficial in the Analysis of Proteins?
title To What Extent is FAIMS Beneficial in the Analysis of Proteins?
title_full To What Extent is FAIMS Beneficial in the Analysis of Proteins?
title_fullStr To What Extent is FAIMS Beneficial in the Analysis of Proteins?
title_full_unstemmed To What Extent is FAIMS Beneficial in the Analysis of Proteins?
title_short To What Extent is FAIMS Beneficial in the Analysis of Proteins?
title_sort to what extent is faims beneficial in the analysis of proteins?
topic Critical Insight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4792363/
https://www.ncbi.nlm.nih.gov/pubmed/26843211
http://dx.doi.org/10.1007/s13361-015-1326-4
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