ArticleJournal of the American Society for Mass Spectrometry2011
Negative ion fragmentation of cysteic acid containing peptides: cysteic acid as a fixed negative charge.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Principles ofbioRxiv : the preprint server for biology · 2026Article
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- The effect of cysteine oxidation on conformational changes of SARS-CoV-2 spike protein using atomistic simulations.Scientific reports · 2025Article
- Aloe Extracellular Vesicles as Carriers of Photoinducible Metabolites Exhibiting Cellular Phototoxicity.Cells · 2024Article
- Identification and Biosynthesis of Pro-Inflammatory Sulfonolipids from an Opportunistic PathogenACS chemical biology · 2022Article
- Atomic-resolution mapping of transcription factor-DNA interactions by femtosecond laser crosslinking and mass spectrometry.Nature communications · 2020Article
- Negative Ion In-Source Decay Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry for Sequencing Acidic Peptides.Journal of the American Society for Mass Spectrometry · 2016Article
- Article
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Authors and funding
5 authors.
Funding
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Abstract
We present here a study of the collision induced dissociation (CID) of deprotonated cysteic acid containing peptides produced by MALDI. The effect of cysteic acid (C(ox)) position is interrogated by considering the positional isomers, C(ox)LVINVLSQG, LVINVLSQGC(ox), and LVINVC(ox)LSQG. Although considerable variation between the CID spectra is observed, the mechanistic picture that emerges involves charge retention at the deprotonated cysteic acid side chain. Fragmentation occurs in the proximity of the cysteic acid group by charge directed mechanisms as well as remote from this group to form ions, which may be rationalized by charge remote mechanisms. Additionally, the formation of the SO(3)(-•) ion is observed in all cases. Fragmentation of C(ox)LVINVLSQC(ox) provides both N- and C-terminal, y and b ions, respectively indicating that the negative charge may be retained at either of the cysteic acids; however, there is some evidence that charge retention at the C-terminal cysteic acid may be preferred. Fragmentation of tryptic type peptides containing a C-terminal arginine or lysine residue is considered through comparison of three peptides C(ox)LVINKLSQG, C(ox)LVINVLSQK, and C(ox)LVINVLSQR. Lastly, we rationalize the formation of b(n-1)+ H(2)O and a(n-1) ions through a mechanism involving rearrangement of the C-terminal residue to form a mixed anhydride intermediate.
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21953265What OpenQuestion holds
Registered trials
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