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''Editing electron-transfer dissociation page for LSU Mass Spec class (Chem 4558) Spring 201'' |
''Editing electron-transfer dissociation page for LSU Mass Spec class (Chem 4558) Spring 201'' |
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'''Electron-transfer dissociation''' (ETD) is a method of [[Fragmentation (mass spectrometry)|fragmenting]] ions in a [[mass spectrometer]] between the stages of [[tandem mass spectrometry]] (MS/MS).<ref>{{Cite book|title=Fundamentals of Contemporary Mass Spectrometry|last=Dass|first=Chhabil|publisher=John Wiley & Sons.|year=2007|isbn=978-0-470-11848-1|location=Hoboken, New Jersey|pages=128}}</ref> Similar to [[electron-capture dissociation]], ETD induces fragmentation of large, multiply-charged [[cations]] by transferring [[electron]]s to them.<ref>{{Cite journal|last=Hart-Smith|first=Gene|date=2014-01-15|title=A review of electron-capture and electron-transfer dissociation tandem mass spectrometry in polymer chemistry|url=http://www.sciencedirect.com/science/article/pii/S000326701301235X|journal=Analytica Chimica Acta|series=Polymer Mass Spectrometry|volume=808|pages=44–55|doi=10.1016/j.aca.2013.09.033}}</ref> ETD is used extensively with large biological molecules such as [[Protein|proteins]] and [[Peptide|peptides]].<ref>{{Cite journal|last=Brodbelt|first=Jennifer S.|date=2015-12-11|title=Ion Activation Methods for Peptides and Proteins|url=http://pubs.acs.org/doi/abs/10.1021/acs.analchem.5b04563|journal=Analytical Chemistry|language=EN|volume=88|issue=1|pages=30–51|doi=10.1021/acs.analchem.5b04563}}</ref> |
'''Electron-transfer dissociation''' (ETD) is a method of [[Fragmentation (mass spectrometry)|fragmenting]] ions in a [[mass spectrometer]] between the stages of [[tandem mass spectrometry]] (MS/MS).<ref>{{Cite book|title=Fundamentals of Contemporary Mass Spectrometry|last=Dass|first=Chhabil|publisher=John Wiley & Sons.|year=2007|isbn=978-0-470-11848-1|location=Hoboken, New Jersey|pages=128}}</ref> Similar to [[electron-capture dissociation]], ETD induces fragmentation of large, multiply-charged [[cations]] by transferring [[electron]]s to them.<ref>{{Cite journal|last=Hart-Smith|first=Gene|date=2014-01-15|title=A review of electron-capture and electron-transfer dissociation tandem mass spectrometry in polymer chemistry|url=http://www.sciencedirect.com/science/article/pii/S000326701301235X|journal=Analytica Chimica Acta|series=Polymer Mass Spectrometry|volume=808|pages=44–55|doi=10.1016/j.aca.2013.09.033}}</ref> ETD is used extensively with large biological molecules such as [[Protein|proteins]] and [[Peptide|peptides]].<ref>{{Cite journal|last=Brodbelt|first=Jennifer S.|date=2015-12-11|title=Ion Activation Methods for Peptides and Proteins|url=http://pubs.acs.org/doi/abs/10.1021/acs.analchem.5b04563|journal=Analytical Chemistry|language=EN|volume=88|issue=1|pages=30–51|doi=10.1021/acs.analchem.5b04563}}</ref> Transferring an electron causes peptide backbone cleavage into [[Peptide sequence tag|c- and z-ions]] while leaving [[Post-translational modification|post translational modifications]] (PTM) intact.<ref>{{Cite journal|last=Coon|first=Joshua J.,|last2=Syka|first2=John E.P.|last3=Shabanowitz|first3=Jeffrey|last4=Hunt|first4=Donald F.|date=April 2005|title=Tandem Mass Spectrometry for Peptide and Protein Sequence Analysis|url=http://www.biotechniques.com/BiotechniquesJournal/2005/April/Tandem-Mass-Spectrometry-for-Peptide-and-Protein-Sequence-Analysis/biotechniques-45438.html|journal=BioTechniques|doi=|pmid=15884666|access-date=April 15, 2016}}</ref> The method was developed by [[Donald F. Hunt]], [[Joshua Coon]], John E. P. Syka and Jarrod Marto at the [[University of Virginia]].<ref>{{US patent reference | number = 7534622 | y = 2009 | m = 05 | d = 19 | inventor = Donald F. Hunt, Joshua J. Coon, John E.P. Syka, Jarrod A. Marto | title = Electron transfer dissociation for biopolymer sequence mass spectrometric analysis}}</ref> |
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[[File:Bruker Amazon Speed ETD.jpg|thumb|320x320px|Bruker Amazon Speed ETD at Louisiana State University]] |
[[File:Bruker Amazon Speed ETD.jpg|thumb|320x320px|Bruker Amazon Speed ETD at Louisiana State University]] |
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New Sandbox for Mass Spec Class
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This is a user sandbox of Kmcke14. You can use it for testing or practicing edits. |
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 between the stages of tandem mass spectrometry (MS/MS).[1] Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them.[2] ETD is used extensively with large biological molecules such as proteins and peptides.[3] Transferring an electron causes peptide backbone cleavage into c- and z-ions while leaving post translational modifications (PTM) intact.[4] The method was developed by Donald F. Hunt, Joshua Coon, John E. P. Syka and Jarrod Marto at the University of Virginia.[5]
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.[6] 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 (CID), resulting in random fragmentation of peptides and proteins.[7] Hunt et. al. set out to create a dissociation method similar to ECD, but using a low-cost, widely available commercial spectrometer. The first ETD experiments were run on a QLT mass spectrometer with an electrospray ionization (ESI) source. [8]
![{\displaystyle [M+nH]^{n+}+A^{-}\to {\bigg [}[M+nH]^{(n-1)+}{\bigg ]}^{*}+A\to fragments}](https://wikimedia.org/api/rest_v1/media/math/render/svg/582715e4ac70599bc9cdcd40ef837e0daeb8cd1a)
.[9]
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newer applications including characterization of PTMs, non-tryptic peptides and intact proteins. (Kim Review)
Textbook[10]
MagLab [11]
Front End ETD (new method - original research)[12]
Proteomics Article (Review)
Performance Characteristics [13]
Book Chapter[14]
Review [15]
new article[16]
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Category:Tandem mass spectrometry
