Differential Ion Mobility-Mass Spectrometry for Detailed Analysis of the Proteome

Daniel L Winter; Marc R Wilkins; William A Donald

doi:10.1016/j.tibtech.2018.07.018

Differential Ion Mobility-Mass Spectrometry for Detailed Analysis of the Proteome

Trends Biotechnol. 2019 Feb;37(2):198-213. doi: 10.1016/j.tibtech.2018.07.018. Epub 2018 Sep 4.

Authors

Daniel L Winter¹, Marc R Wilkins¹, William A Donald²

Affiliations

¹ School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales, 2052, Australia.
² School of Chemistry, University of New South Wales, Sydney, New South Wales, 2052, Australia. Electronic address: w.donald@unsw.edu.au.

PMID: 30193737
DOI: 10.1016/j.tibtech.2018.07.018

Abstract

The field of proteomics is increasingly concerned with the diversity and functional relevance of protein modifications. Differential ion mobility spectrometry (DMS) is emerging as a tool to detect and quantify additional peptide and protein species that are difficult to analyse with conventional instrumental methods. In this review, recent advances in DMS are discussed, with a focus on the different types of DMS instruments now available to researchers in proteomics. Furthermore, the combination of DMS with mass spectrometry (MS) for increased proteome coverage and the targeted analysis of modification patterns on single proteins is highlighted. Frontier areas of research, such as the analysis of intact proteoforms, and future directions for the implementation of DMS in proteomics are also discussed.

Keywords: differential ion mobility spectrometry; ion mobility; mass spectrometry; proteomics; systems biology.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Ion Mobility Spectrometry / methods*
Mass Spectrometry / methods*
Proteins / analysis*
Proteome / analysis*

Substances

Proteins
Proteome