Unique Fragmentation of DEST Cross-Linked Peptides Facilitates Their Identification

摘要

Singly-charged, collisionally activated DEST cross-linked peptides were found to undergo preferential cleavage at cross-linking sites. Intense peaks for alpha+XL and beta+XL product ions were observed in most cases. The intensities of alpha+XL and beta+XL are mainly dependent on the basicities of the individual peptide chains. A new algorithm was developed for the facile identification of cross-links based on this unique fragmentation propensity.