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• W2000601864 abstract "We present a novel approach for the assignment of peptides containing disulfide linkages. Dimethyl labeling is introduced to generate labeled peptides which exhibit enhanced a1 ion signals during MS/MS fragmentation. For disulfide-linked peptides, multiple a1 ions can be observed due to multiple N-termini. This distinct feature allows sieving out the disulfide-linked peptides; meanwhile, the N-terminal amino acids can be identified. With such information, the number of possible peptide combinations involved in a disulfide bond dramatically narrows down. Furthermore, we developed a computational algorithm to perform target a1 ion screening followed by molecular weight matching of cysteine-containing peptides with specific amino acids at the N-termini. Once the protein sequence and the peak list from a LC−MS/MS survey scan of labeled peptides are imported, the identities of disulfide-linked peptides can be readily obtained. The presented approach is simple and straightforward, offering a valuable tool for protein structural characterization." @default.
• W2000601864 created "2016-06-24" @default.
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• W2000601864 date "2008-11-07" @default.
• W2000601864 modified "2023-10-17" @default.
• W2000601864 title "Assignment of Disulfide-Linked Peptides Using Automatic a₁ Ion Recognition" @default.
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• W2000601864 doi "https://doi.org/10.1021/ac8013725" @default.
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