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Modelling of the gas‐phase phosphate group loss and rearrangement in phosphorylated peptides
Author(s) -
Rožman Marko
Publication year - 2011
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1835
Subject(s) - chemistry , fragmentation (computing) , phosphopeptide , phosphorylation , tandem mass spectrometry , dissociation (chemistry) , gas phase , mass spectrometry , phosphate , collision induced dissociation , context (archaeology) , protein phosphorylation , tandem , chromatography , biochemistry , organic chemistry , protein kinase a , paleontology , materials science , computer science , composite material , biology , operating system
Phosphorylation is a key reversible protein posttranslational modifi cation that regulates enzymatic activity, subcellular localization, complex formation and degradation of proteins. Over the past several years, advances in mass spectrometry instrumentation coupled to the development of analytical methods have allowed investigation of the phosphoproteome on a global scale. The molecular modeling work presented in this special feature article provides insight into the energetic and kinetic aspects of the gas‐phase unimolecular dissociation of phosphorylated peptides. During phosphorylation analysis by CID tandem MS, some gas‐phase chemistry issues are causing diffi culties in proper sequence assignments, and consensus concerning the gas‐phase fragmentation pathways for phosphate loss has not yet been reached. Therefore, elucidation of the proper phosphopeptide fragmentation behavior is of high importance in the context of predicting tandem MS ion abundances. Marko Rozman (Ph.D.) is a talented research associate in the Laboratory for chemical kinetics and atmospheric chemistry of the Ruder Boskovic Institue in Zagreb Croatia with strong interests in modeling gas phase ion structures and fragmentation reactions.