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.
Marko Rožman obtained his PhD in physical chemistry at the University of Zagreb working on the gas-phase structure and reactivity of cationized amino acids. He conducted postdoctoral research in analytical mass spectrometry at the Jožef Stefan Institute (Ljubljana) followed by second postdoctoral appointment at the Simon Gaskell's group (University of Manchester). MR is currently working as a research associate at the Ruđer Bošković Institute, Zagreb, Croatia. His current research focuses on properties, reactions, and structures of biologically relevant molecules in the gas phase as well as on developing new experimental strategies for peptide/protein analysis.