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• W2322983019 endingPage "6133" @default.
• W2322983019 startingPage "6123" @default.
• W2322983019 abstract "Peptide radical cations AnY•+ (where n = 3, 4, or 5) and A5W•+ have been generated by collision-induced dissociation (CID) of [CuII(tpy)(peptide)]•2+ complexes. Apart from the charge-driven fragmentation at the N–Cα bond of the hetero residue producing either [c + 2H]+ or [z – H]•+ ions and radical-driven fragmentation at the Cα–C bond to give a+ ions, unusual product ions [x + H]•+ and [z + H]•+ are abundant in the CID spectra of the peptides with the hetero residue in the second or third position of the chain. The formation of these ions requires that both the charge and radical be located on the peptide backbone. Energy-resolved spectra established that the [z + H]•+ ion can be produced either directly from the peptide radical cation or via the fragment ion [x + H]•+. Additionally, backbone dissociation by loss of the C-terminal amino acid giving [b(n–1) – H]•+ increases in abundance with the length of the peptides. Mechanisms by which peptide radical cations dissociate have been modeled using density functional theory (B3LYP/6-31++G** level) on tetrapeptides AYAG•+, AAYG•+, and AWAG•+." @default.
• W2322983019 created "2016-06-24" @default.
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• W2322983019 date "2014-05-29" @default.
• W2322983019 modified "2023-10-16" @default.
• W2322983019 title "Fragmentation of Peptide Radical Cations Containing a Tyrosine or Tryptophan Residue: Structural Features That Favor Formation of [<i>x</i>_{(<i>n</i>–1)} + H]^•+ and [<i>z</i>_{(<i>n</i>–1)} + H]^•+ Ions" @default.
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• W2322983019 doi "https://doi.org/10.1021/jp5030087" @default.
• W2322983019 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24823970" @default.
• W2322983019 hasPublicationYear "2014" @default.
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