Fragmentation of multiply-charged intact protein ions using MALDI TOF-TOF mass spectrometry.

ABSTRACT: Top down proteomics in a TOF-TOF instrument was further explored by examining the fragmentation of multiply charged precursors ions generated by matrix-assisted laser desorption ionization. Evaluation of sample preparation conditions allowed selection of solvent/matrix conditions and sample deposition methods to produce sufficiently abundant doubly and triply charged precursor ions for subsequent CID experiments. As previously reported, preferential cleavage was observed at sites C-terminal to acidic residues and N-terminal to proline residues for all ions examined. An increase in nonpreferential fragmentation as well as additional low mass product ions was observed in the spectra from multiply charged precursor ions providing increased sequence coverage. This enhanced fragmentation from m

SUBMITTER: Liu Z 

PROVIDER: S-EPMC2288703 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature