title: Unique fragmentation of singly charged DEST cross-linked peptides.
abstract: It has previously been shown that when cross-linking reagent diethyl suberthioimidate (DEST) reacts with primary amines of proteins to yield amidinated residues, the primary amines retain their high basicity, and cross-linked species can be enriched by strong cation exchange. It is now demonstrated that collisional activation of singly-charged DEST cross-linked peptide ions leads to preferential cleavage at the cross-linked sites. The resulting product ions facilitate the detection and identification of cross-linked peptides.
authors.affiliation: Indiana University, Bloomington, IN, USA.
authors.forename: Yi
authors.initials: Y
authors.lastname: He
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Lauber
authors.forename: James P
authors.initials: JP
authors.lastname: Reilly
mesh_terms: D003432:Cross-Linking Reagents / Q000737:chemistry; D007477:Ions / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
chemical_list: D003432:Cross-Linking Reagents; D007477:Ions; D010455:Peptides