Collision-induced reporter fragmentations for identification of covalently modified peptides.
Collision-induced reporter fragmentations of the currently most important covalent peptide modifications as detected by tandem mass spectrometry are summarized. These fragmentations comprise the formation of reporter ions, which are preferentially immonium ions, immonium ion-derived fragments or side chain fragments. In addition, the reporter neutral loss reactions for covalently modified amino acid residues are summarized. For each individual covalent modification which can be recognized by a reporter fragmentation, the accurate mass shift and the gross formula shift of the modified amino acid residue are given. The same set of data is provided for the reporter fragmentations. Finally, an extensive accurate mass and gross formula list is presented as supplementary material, describing mostly regular and modified y(1) and dipeptide a and b ions, which are helpful for identification of the peptide ends of covalently modified peptides.
Hung
Chien-Wen
CW
Molecular Structure Analysis, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120, Heidelberg, Germany.
Schlosser
Andreas
A
Wei
Junhua
J
Lehmann
Wolf D
WD
D000596:Amino Acids / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis* / Q000737:chemistry; D046188:Protein Modification, Translational; D011506:Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D020543:Proteome / Q000032:analysis; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*
D000596:Amino Acids; D010446:Peptide Fragments; D011506:Proteins; D020543:Proteome