Electron Transfer Dissociation (ETD)

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 Thermo Scientific™ Orbitrap™ Tribrid™ mass spectrometers. Thermo Scientific™ Proteome Discoverer™ and Thermo Scientific™ BioPharma Finder™ software includes unique capabilities to help users take full advantage of the information provided by ETD. Our systems also are capable of serializing ETD reactions with EThcD or ETciD collisional-based fragmentation, which enables researchers to add minimal collisional energy to the ETD reaction to assist in fragmentation release after ETD. Thermo Scientific software is capable of analyzing and reading this unique combination technique.

• 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 charge reduction (PTCR) 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 Orbitrap Tribrid 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