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ETD provides sequence information not available from conventional methods used in ion trap mass spectrometers
ETD enables peptide dissociation by transferring electrons to positively charged peptides, leading to a rich ladder of sequence ions derived from cleavage at the amide groups along the peptide backbone. Amino acid side chains and important modifications such as phosphorylation are preserved intact and can be readily assigned as a result of analysis.
The ETD source exploits the open architecture of the LTQ and is physically coupled to the back-end of the two-dimensional ion trap. The electrospray source remains on the front-end of the system. This flexible design allows for the future addition of other ion reaction types (such as PTR).
Since large peptides can be successfully fragmented by ETD, this upgrade enables top-down and middle-down sequencing of small proteins/large peptides and supports bottom-up proteomics using enzymes that make larger peptide fragments.
Using ETD technology, your research will benefit from:
- Enhanced protein identification and sequence coverage using bottom-up approaches
- Improved identification of the location of post-translational modifications
- Enhanced MS/MS of basic peptides and proteins such as histones
- Much improved sequencing by MS/MS of large peptides and proteins
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