Electron Capture Dissociation Mass Spectrometry in Characterization of Peptides and Proteins
- First Online:
Electron capture dissociation (ECD) represents one of the most recent and significant advancements in tandem mass spectrometry (MS/MS) for the identification and characterization of polypeptides. In comparison with the conventional fragmentation techniques, such as collisionally activated dissociation (CAD), ECD provides more extensive sequence fragments, while allowing the labile modifications to remain intact during backbone fragmentation—an important attribute for characterizing post-translational modifications. Herein, we present a brief overview of the ECD technique as well as selected applications in characterization of peptides and proteins. Case studies including characterization and localization of amino acid glycosylation, methionine oxidation, acylation, and “top–down” protein mass spectrometry using ECD will be presented. A recent technique, coined as electron transfer dissociation (ETD), will be also discussed briefly.
Key wordsElectron capture dissociation Electron transfer dissociation Electrospray ionization Fourier transform mass spectrometry Post-translational modifications
Unable to display preview. Download preview PDF.
- Borchers CH, Thapar R, Petrotchenko EV, Torres MP, Speir JP, Easterling M, Dominski Z, Marzluff WF (2006) Combined top–down and bottom–up proteomics identifies a phsophorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding. Proc Natl Acad Sci USA 103:3094–3099PubMedCrossRefGoogle Scholar
- Medzihradszky KF, Zhang X, Chalkley RJ, Guan S, McFarland MA, Chalmers MJ, Marshall AG, Diaz RL, Allis CD, Burlingame AL (2004) Characterization of Tetrahymena Histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS). Mol Cell Proteomics 3:872–886PubMedCrossRefGoogle Scholar
- Nemeth-Cawley JF, Tangarone BS, Rouse JC (2003) “Top down” characterization is a complementary technique to peptide sequencing for identifying protein species in complex mixtures. J Proteomics 2:495–505Google Scholar
- Savitski MM, Nielsen ML, Zubarev RA (2005) New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse score, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques. Mol Cell Proteomics 4:1180–1188PubMedCrossRefGoogle Scholar