4.7 Review

Ion mobility mass spectrometry for peptide analysis

Journal

METHODS
Volume 54, Issue 4, Pages 454-461

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2011.05.004

Keywords

-

Funding

  1. EPSRC
  2. BBSRC
  3. British Mass Spectrometry Society
  4. BBSRC [BB/H013636/1] Funding Source: UKRI
  5. EPSRC [EP/E030173/1] Funding Source: UKRI
  6. Biotechnology and Biological Sciences Research Council [BB/H013636/1] Funding Source: researchfish
  7. Engineering and Physical Sciences Research Council [GR/S77639/01, EP/E030173/1] Funding Source: researchfish

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available