ArticleJournal of the American Society for Mass Spectrometry2013
157 nm photodissociation of a complete set of dipeptide ions containing C-terminal arginine.
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 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Bond-specific fragmentation of oligopeptides via electronic stopping of swift heavy ions in molecular films.Scientific reports · 2022Article
- Unusual fragmentation of derivatized cysteine-containing peptides.Rapid communications in mass spectrometry : RCM · 2018Article
- A Novel Triethylphosphonium Charge Tag on Peptides: Synthesis, Derivatization, and Fragmentation.Journal of the American Society for Mass Spectrometry · 2017Article
- Statistical Examination of the a and a + 1 Fragment Ions from 193 nm Ultraviolet Photodissociation Reveals Local Hydrogen Bonding Interactions.Journal of the American Society for Mass Spectrometry · 2016Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2016Review
- Charge transfer dissociation (CTD) mass spectrometry of peptide cations using kiloelectronvolt helium cations.Journal of the American Society for Mass Spectrometry · 2014Article
- Photodissociation mass spectrometry: new tools for characterization of biological molecules.Chemical Society reviews · 2014Review
- 157 nm photodissociation of dipeptide ions containing N-terminal arginine.Journal of the American Society for Mass Spectrometry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Twenty singly-charged dipeptide ions with C-terminal arginine were photodissociated with 157 nm light and their tandem mass spectra recorded. Many of the small product ions that were observed are standard peptide fragments that have been commonly seen in VUV photodissociation studies. However, the study of a library of dipeptides containing all 20 N-terminal amino acids enabled the recognition of trends associated with the occurrence of w-, v-, and immonium ions, the observation of competition between forming N- and C-terminal fragments in dipeptide RR, and the identification of some unusual fragment ions appearing at masses of 183, 187, 196, and 197 Da. A highly accurate internal calibration of the photodissociation TOF-TOF data enabled molecular formulae for these four product ions to be derived. Their proposed structures reflect the rather high-energy nature of this fragmentation phenomenon.
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Registered trials
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