ArticleJournal of the American Society for Mass Spectrometry2013
Characterization of electron transfer dissociation in the Orbitrap Velos HCD cell.
Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Modified Ion Source for the Improved Collisional Activation of Protein Complexes.Journal of the American Society for Mass Spectrometry · 2023Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- A calibration routine for efficient ETD in large-scale proteomics.Journal of the American Society for Mass Spectrometry · 2015Article
- Hybridizing ultraviolet photodissociation with electron transfer dissociation for intact protein characterization.Analytical chemistry · 2014Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electron transfer dissociation (ETD) is commonly employed in ion traps utilizing rf fields that facilitate efficient electron transfer reactions. Here, we explore performing ETD in the HCD collision cell on an Orbitrap Velos instrument by applying a static DC gradient axially to the rods. This gradient enables simultaneous three dimensional, charge sign independent, trapping of cations and anions, initiating electron transfer reactions in the center of the HCD cell where oppositely charged ions clouds overlap. Here, we evaluate this mode of operation for a number of tryptic peptide populations and the top-down sequence analysis of ubiquitin. Our preliminary data show that performing ETD in the HCD cell provides similar fragmentation as ion trap-ETD but requires further optimization to match performance of ion trap-ETD.
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Registered trials
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