3C-O1-0915（3P-34） PDF
High-energy electron transfer dissociation (HE-ETD) of protonated disulfide linked peptides with high-resolution tandem Time-of-flight mass spectrometer
Disulfide linkages in polypeptides are post-translational modifications that play a pivotal role in maintaining higher order structure and biological functions. In this work, high-energy electron transfer dissociation (HE-ETD) using Cs targets was applied to doubly protonated disulfide linked polypeptides, such as vasopressin and vasotocin. From both cleavage of peptide bond and S-S bond, it was found that the peptide sequence having S-S bond was able to be completely determined by HE-ETD spectra. C-S bond of the cysteine residue in the central part cleaved easier than that in the N-terminal.