Electron transfer dissociation mass spectrometry in proteomics

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‐translation...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2012-02, Vol.12 (4-5), p.530-542
Main Authors: Kim, Min-Sik, Pandey, Akhilesh
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
ETD
Fundamental and applied biological sciences. Psychology
Ions
Mass spectrometry
Mass Spectrometry - methods
Miscellaneous
MRM
Non-tryptic peptide
O-GlcNAc
Peptides - chemistry
Peptides - metabolism
Protein Modification, Translational
Proteins
Proteins - metabolism
Proteogenomics
Proteomics
Proteomics - methods
Sequence Analysis, Protein - methods
Technology
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Summary: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.
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.201100517