New Sandbox for Mass Spec Class
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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]
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.
ETD does not use free electrons but employs radical anions (e.g. anthraceneorazobenzene) for this purpose:
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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]
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Category:Tandem mass spectrometry