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.
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