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Published on: November 15, 2017
Electron transfer dissociation mass spectrometry in proteomics
1Department of Biological Chemistry, McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Proteomics
|January 17, 2012
Summary
Electron Transfer Dissociation (ETD) complements Collision-Induced Dissociation (CID) for advanced proteomic analysis. This review covers ETD
Area of Science:
- Proteomics
- Analytical Chemistry
- Biochemistry
Background:
- Mass spectrometry is the leading platform for proteomic analysis.
- Collision-Induced Dissociation (CID) is the standard for peptide sequencing.
- Electron Transfer Dissociation (ETD) offers complementary fragmentation capabilities.
Purpose of the Study:
- To review the evolution and applications of Electron Transfer Dissociation (ETD).
- To highlight ETD's utility in characterizing post-translational modifications (PTMs), non-tryptic peptides, and intact proteins.
- To discuss ETD's unique features, data analysis challenges, and future potential.
Main Methods:
- Review of existing literature on ETD.
- Comparative analysis of ETD and CID fragmentation techniques.
- Discussion of novel applications and future directions in proteomic analysis.
Main Results:
- ETD is an emerging complementary method to CID for peptide and post-translational modification (PTM) characterization.
- ETD enables detailed analysis of PTMs, non-tryptic peptides, and intact proteins.
- Alternating CID/ETD strategies offer enhanced analytical power.
Conclusions:
- ETD significantly expands the capabilities of mass spectrometry in proteomics.
- Future applications of ETD include multiple reaction monitoring and proteogenomics.
- ETD is crucial for comprehensive proteomic and PTM analysis.
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