Electron-capture dissociation tandem mass spectrometry
- PMID: 15102460
- DOI: 10.1016/j.copbio.2003.12.002
Electron-capture dissociation tandem mass spectrometry
Abstract
Electron capture dissociation (ECD) is a new fragmentation technique used in Fourier transform ion cyclotron resonance mass spectrometry and is complementary to traditional tandem mass spectrometry techniques. Disulfide bonds, normally stable to vibrational excitation, are preferentially cleaved in ECD. Fragmentation is fast and specific and labile post-translational modifications and non-covalent bonds often remain intact after backbone bond dissociation. ECD provides more extensive sequence coverage in polypeptides, and at higher electron energies even isoleucine and leucine are distinguishable. In biotechnology, the main area of ECD application is expected to be the top-down verification of DNA-predicted protein sequences, de novo sequencing, disulfide bond analysis and the combined top-down/bottom-up analysis of post-translational modifications.
Similar articles
-
Protein primary structure using orthogonal fragmentation techniques in Fourier transform mass spectrometry.Expert Rev Proteomics. 2006 Apr;3(2):251-61. doi: 10.1586/14789450.3.2.251. Expert Rev Proteomics. 2006. PMID: 16608437 Review.
-
Electron capture dissociation mass spectrometry in characterization of post-translational modifications.Biochem Biophys Res Commun. 2005 Aug 19;334(1):1-8. doi: 10.1016/j.bbrc.2005.05.138. Biochem Biophys Res Commun. 2005. PMID: 15950932 Review.
-
Peptide and protein characterization by high-rate electron capture dissociation Fourier transform ion cyclotron resonance mass spectrometry.J Mass Spectrom. 2004 Jul;39(7):719-29. doi: 10.1002/jms.658. J Mass Spectrom. 2004. PMID: 15282750
-
The role of electron capture dissociation in biomolecular analysis.Mass Spectrom Rev. 2005 Mar-Apr;24(2):201-22. doi: 10.1002/mas.20014. Mass Spectrom Rev. 2005. PMID: 15389856 Review.
-
Combined infrared multiphoton dissociation and electron capture dissociation with a hollow electron beam in Fourier transform ion cyclotron resonance mass spectrometry.Rapid Commun Mass Spectrom. 2003;17(15):1759-68. doi: 10.1002/rcm.1118. Rapid Commun Mass Spectrom. 2003. PMID: 12872281
Cited by
-
Improving Peptide identification using empirical scoring systems.Methods Mol Biol. 2013;1007:173-82. doi: 10.1007/978-1-62703-392-3_7. Methods Mol Biol. 2013. PMID: 23666726 Free PMC article.
-
Enhanced electron transfer dissociation of peptides modified at C-terminus with fixed charges.J Am Soc Mass Spectrom. 2012 Nov;23(11):1991-2000. doi: 10.1007/s13361-012-0458-z. Epub 2012 Aug 16. J Am Soc Mass Spectrom. 2012. PMID: 22895859
-
Selectivity over coverage in de novo sequencing of IgGs.Chem Sci. 2020 Oct 6;11(43):11886-11896. doi: 10.1039/d0sc03438j. eCollection 2020 Nov 21. Chem Sci. 2020. PMID: 33520151 Free PMC article.
-
Meta-heterogeneity: Evaluating and Describing the Diversity in Glycosylation Between Sites on the Same Glycoprotein.Mol Cell Proteomics. 2021;20:100010. doi: 10.1074/mcp.R120.002093. Epub 2020 Dec 8. Mol Cell Proteomics. 2021. PMID: 33561609 Free PMC article. Review.
-
Sequential abundant ion fragmentation analysis (SAIFA): an alternative approach for phosphopeptide identification using an ion trap mass spectrometer.Anal Biochem. 2011 Nov 15;418(2):197-203. doi: 10.1016/j.ab.2011.07.026. Epub 2011 Jul 30. Anal Biochem. 2011. PMID: 21855524 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources