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1 History  





2 Principle of operation  





3 Instrumentation  





4 Proteomics  





5 Changes to the method  





6 See also  





7 References  














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< User:Kmcke14

This is an old revision of this page, as edited by Kmcke14 (talk | contribs)at00:46, 15 April 2016 (spacing). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.
(diff)  Previous revision | Latest revision (diff) | Newer revision  (diff)

New Sandbox for Mass Spec Class

Editing electron-transfer dissociation page for LSU Mass Spec class (Chem 4558) Spring 201

Electron-transfer dissociation (ETD) is a method of fragmenting ions in a mass spectrometer.[1] Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them.[2] Because it is a relatively low-energy fragmentation method ETD is used extensively with large biological molecules such as proteins and peptides.[3] The method was developed by Donald F. Hunt, Joshua Coon, John E. P. Syka and Jarrod Marto at the University of Virginia.[4]

Bruker Amazon Speed ETD at Louisiana State University

History

Because electron-capture dissociation (ECD) requires a large amount of near-thermal electrons (<0.2eV), originally it was used exclusively with Fourier transform ion cyclotron resonance mass spectrometry (FTICR), the most expensive form of MS instrumentation.[5] Less costly options such as quadrupole time-of-flight (Q-TOF), quadrupole ion trap (QIT) and linear quadrupole ion trap (QLT) instruments used the more energy-intensive collision-activated dissociation method (CAD), resulting in random fragmentation of peptides and proteins.[6] Hunt et. al. set out to create a dissociation method similar to ECD, but using a low-cost, widely available spectrometer like QLT or Q-TOF for protein sequence analysis.

Principle of operation

ETD does not use free electrons but employs radical anions (e.g. anthraceneorazobenzene) for this purpose:

.[7]
where A is the anion. ETD cleaves randomly along the peptide backbone (so called c and z ions) while side chains and modifications such as phosphorylation are left intact. The technique only works well for higher charge state ions (z>2), however relative to collision-induced dissociation (CID), ETD is advantageous for the fragmentation of longer peptides or even entire proteins. This makes the technique important for top-down proteomics.
Peptide Fragmentation

Instrumentation

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Bruker high capacity ion trap with ETD (schematic diagram) 

Proteomics

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Changes to the method

newer applications including characterization of PTMs, non-tryptic peptides and intact proteins. (Kim Review)

Textbook[8]

MagLab [9]

Front End ETD (new method - original research)[10]

Proteomics Article (Review)

Performance Characteristics [11]

Book Chapter[12]

Review [13]

new article[14]

See also

References

  1. ^ Dass, Chhabil (2007). Fundamentals of Contemporary Mass Spectrometry. Hoboken, New Jersey: John Wiley & Sons. p. 128. ISBN 978-0-470-11848-1.
  • ^ Hart-Smith, Gene (2014-01-15). "A review of electron-capture and electron-transfer dissociation tandem mass spectrometry in polymer chemistry". Analytica Chimica Acta. Polymer Mass Spectrometry. 808: 44–55. doi:10.1016/j.aca.2013.09.033.
  • ^ Brodbelt, Jennifer S. (2015-12-11). "Ion Activation Methods for Peptides and Proteins". Analytical Chemistry. 88 (1): 30–51. doi:10.1021/acs.analchem.5b04563.
  • ^ US patent 7534622, Donald F. Hunt, Joshua J. Coon, John E.P. Syka, Jarrod A. Marto, "Electron transfer dissociation for biopolymer sequence mass spectrometric analysis", issued 2009-05-19 
  • ^ McLafferty, Fred W.; Horn, David M.; Breuker, Kathrin; Ge, Ying; Lewis, Mark A.; Cerda, Blas; Zubarev, Roman A.; Carpenter, Barry K. (2001-03-01). "Electron capture dissociation of gaseous multiply charged ions by Fourier-transform ion cyclotron resonance". Journal of the American Society for Mass Spectrometry. 12 (3): 245–249. doi:10.1016/S1044-0305(00)00223-3. ISSN 1044-0305.
  • ^ Syka JE, Coon JJ, Schroeder MJ, Shabanowitz J, Hunt DF (2004). "Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 101 (26): 9528–33. Bibcode:2004PNAS..101.9528S. doi:10.1073/pnas.0402700101. PMC 470779. PMID 15210983.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • ^ McLuckey SA, Stephenson JL (1998). "Ion/ion chemistry of high-mass multiply charged ions". Mass spectrometry reviews. 17 (6): 369–407. doi:10.1002/(SICI)1098-2787(1998)17:6<369::AID-MAS1>3.0.CO;2-J. PMID 10360331.
  • ^ Dass, Chhabil (2007). Fundamentals of Contemporary Mass Spectromrtry. Hoboken, N.J.: John Wiley ^ Sons, Inc. ISBN 978-0-471-68229-5.
  • ^ "Electron Transfer Dissociation - MagLab". nationalmaglab.org. Retrieved 2016-03-01.
  • ^ Earley, Lee; Anderson, Lissa C.; Bai, Dina L.; Mullen, Christopher; Syka, John E. P.; English, A. Michelle; Dunyach, Jean-Jacques; Stafford, George C.; Shabanowitz, Jeffrey (2013-08-19). "Front-End Electron Transfer Dissociation: A New Ionization Source". Analytical Chemistry. 85 (17): 8385–8390. doi:10.1021/ac401783f. PMC 3822909. PMID 23909443.
  • ^ Good, David M.; Wirtala, Matthew; McAlister, Graeme C.; Coon, Joshua J. (2007-11-01). "Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry". Molecular & Cellular Proteomics. 6 (11): 1942–1951. doi:10.1074/mcp.M700073-MCP200. ISSN 1535-9476. PMID 17673454.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • ^ Elviri, Lisa (2012-02-29). ETD and ECD Mass Spectrometry Fragmentation for the Characterization of Protein Post Translational Modifications. InTech. doi:10.5772/35277.
  • ^ Zhang, Zhaorui; Wu, Si; Stenoien, David L.; Paša-Tolić, Ljiljana (2014-01-01). "High-Throughput Proteomics". Annual Review of Analytical Chemistry. 7 (1): 427–454. doi:10.1146/annurev-anchem-071213-020216. PMID 25014346.
  • ^ Nilsson, Jonas (2016-01-18). "Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides". Glycoconjugate Journal: 1–12. doi:10.1007/s10719-016-9649-3. ISSN 0282-0080.

  • Category:Tandem mass spectrometry


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    This page was last edited on 15 April 2016, at 00:46 (UTC).

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