A review of the collision‐induced dissociations of deprotonated dipeptides and tripeptides. An aid to structure determination

The structures of underivatized di‐ and tripeptides may be determined from a consideration of the collision‐induced dissociations of their [M—H] − ions. There are three types of fragmentation, viz. (i) the backbone cleavage which provides sequencing information, (ii) α side‐chain cleavage irrespective of the position of the amino acid residue, and (iii) cleavages which are characteristic of amino acid residues in specific positions, in particular the N‐ or C‐terminal positions.