Ion mobility mass spectrometry for peptide analysis

Sophie R. Harvey, Cait E. MacPhee, Perdita E. Barran

Research output: Contribution to journalLiterature reviewpeer-review

Abstract / Description of output

The use of ion mobility mass spectrometry has grown rapidly over the last two decades. This powerful analytical platform now forms an attractive prospect for comprehensive analysis of many different molecular species, including chemically complex biological molecules. This paper describes the application of IM-MS to the study of peptides. We focus on three different ion mobility devices that are most frequently found in tandem with mass spectrometers. These are instruments using linear drift tubes (LDT), those using travelling wave ion guides (TWIGS) and those employing high field asymmetric ion mobility spectrometry (FAIMS). Each technique is described. Examples are given on the use of IM-MS for the determination of peptide structure, the study of peptides that form amyloid fibrils, and the study of complex peptide mixtures in proteomic investigations. We describe and comment on the methodologies used and the outlook for this developing analytical technique. (C) 2011 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)454-461
Number of pages8
JournalMethods in Molecular Biology
Volume54
Issue number4
DOIs
Publication statusPublished - Aug 2011

Keywords / Materials (for Non-textual outputs)

  • GAS-PHASE MEASUREMENTS
  • OF-FLIGHT TECHNIQUES
  • ESI-FAIMS-MS
  • ELECTROSPRAY-IONIZATION
  • ATMOSPHERIC-PRESSURE
  • TRYPTIC PEPTIDES
  • CONFORMATIONAL PREFERENCES
  • DROSOPHILA-MELANOGASTER
  • PROTEIN COMPLEXES
  • DRIFT-TUBE

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