ArticleJournal of the American Society for Mass Spectrometry2009
On the charge partitioning between c and z fragments formed after electron-capture induced dissociation of charge-tagged Lys-Lys and Ala-Lys dipeptide dications.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- Investigation of the Mechanism of Electron Capture and Electron Transfer Dissociation of Peptides with a Covalently Attached Free Radical Hydrogen Atom Scavenger.International journal of mass spectrometry · 2015Article
- Electron transfer dissociation of photolabeled peptides. Backbone cleavages compete with diazirine ring rearrangements.Journal of the American Society for Mass Spectrometry · 2013Article
- The early life of a peptide cation-radical. Ground and excited-state trajectories of electron-based peptide dissociations during the first 330 femtoseconds.Journal of the American Society for Mass Spectrometry · 2012Article
- Unusual fragmentation of β-linked peptides by ExD tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Formation of peptide radical cations (m+·) in electron capture dissociation of peptides adducted with group IIB metal ions.Journal of the American Society for Mass Spectrometry · 2011Article
- Electron-capture and -transfer dissociation of peptides tagged with tunable fixed-charge groups: structures and dissociation energetics.Journal of the American Society for Mass Spectrometry · 2011Article
- The relative charge ratio between C and N atoms in amide bond acts as a key factor to determine peptide fragment efficiency in different charge states.Journal of the American Society for Mass Spectrometry · 2010Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here we report on the charge partition between c and z fragments formed after femtosecond collisional electron-transfer from Cs atoms to charge-tagged peptide dications. Peptides chosen for study were Ala-Lys (AK) and Lys-Lys (KK) where one or both of the lysine epsilon-amino groups were trimethylated to provide one or two fixed charges. For peptides with only one charge tag, the other charge was obtained by protonation of an amino group. In some experiments the ammonium group was tagged by 18-crown-6-ether (CE). Since recombination energies decrease in the order: MeNH3+ > NMe4+ > MeNH3+(CE) > NMe4+(CE), it is possible to change the probability for the transferred electron to end up at either the N-terminal or the C-terminal residue by CE attachment. We find, however, that the individual recombination energies have little influence on the relative ratio between the yield of c and z ions as long as there are no mobile protons that can be transferred between the two fragments. Our results can be accounted for by the Utah-Washington model where the electron is captured into an amide pi* orbital that weakens the N-C(alpha) bond and causes its breakage, followed by proton, electron, or hydrogen transfer between the c and z fragments that stay together as an ion-molecule complex for some time. The data are also in accordance with the notion that an amide group competes with the charged groups for the electron. Electron capture by charged groups results in loss of small neutrals such as hydrogen and ammonia.
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