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Proteomics. 2012 Feb;12(4-5):530-42. doi: 10.1002/pmic.201100517. Epub 2012 Jan 23.

Electron transfer dissociation mass spectrometry in proteomics.

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1
Department of Biological Chemistry, McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

Abstract

Mass spectrometry has rapidly evolved to become the platform of choice for proteomic analysis. While CID remains the major fragmentation method for peptide sequencing, electron transfer dissociation (ETD) is emerging as a complementary method for the characterization of peptides and post-translational modifications (PTMs). Here, we review the evolution of ETD and some of its newer applications including characterization of PTMs, non-tryptic peptides and intact proteins. We will also discuss some of the unique features of ETD such as its complementarity with CID and the use of alternating CID/ETD along with issues pertaining to analysis of ETD data. The potential of ETD for applications such as multiple reaction monitoring and proteogenomics in the future will also be discussed.

PMID:
22246976
PMCID:
PMC3664229
DOI:
10.1002/pmic.201100517
[Indexed for MEDLINE]
Free PMC Article
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