Thermo Scientific™

Electron Transfer Dissociation (ETD)

Related applications:

Industrial Mass Spectrometry

Achieve better analysis of proteins and their post-translational modifications (PTMs) with the Thermo Scientific™ Electron Transfer Dissociation (ETD) option. Unlike CID, which cleaves weakly bound modifications off the peptide backbone, ETD induces fragmentation along the peptide backbone in a sequence-independent manner, leaving labile modifications linked to the peptide chain. This greatly simplifies identification of modification sites. ETD produces primarily c- and z-type fragment ions that complement the b- and y-type ions produced by CID, increasing sequence coverage and protein IDs.
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Electron transfer dissociation is a supremely useful tool for the analysis of post-translationally modified proteins. ETD capability can be added to many Thermo Scientific™ ion trap and Orbitrap™ mass spectrometers. Thermo Scientific™ Proteome Discoverer™ software includes unique capabilities to help users take full advantage of the information provided by ETD.
  • ETD preserves labile PTMs, allowing straightforward identification of the peptide sequence and the site of modification
  • For top-down analysis, ETD can be combined with proton transfer reaction (PTR) which dramatically simplifies spectra from intact proteins
  • For workflows that include low-mass isobaric mass tags, ETD can be combined with pulsed-Q dissociation (PQD) which eliminates the normal low-mass cutoff
  • ETD can be added to most Thermo Scientific LTQ-series ion trap and hybrid ion trap-Orbitrap mass spectrometers
  • Proteome Discoverer software includes the proprietary Z-Core database search algorithm specifically optimized for ETD spectra
  • Proteome Discoverer software can easily merge complementary CID and ETD results to maximize protein sequence coverage