Sequencing Larger Intact Proteins (30-70 kDa) with Activated Ion Electron Transfer Dissociation.

ABSTRACT: The analysis of intact proteins via mass spectrometry can offer several benefits to proteome characterization, although the majority of top-down experiments focus on proteoforms in a relatively low mass range (<30 kDa). Recent studies have focused on improving the analysis of larger intact proteins (up to ~75 kDa), but they have also highlighted several challenges to be addressed. One major hurdle is the efficient dissociation of larger protein ions, which often to do not yield extensive fragmentation via conventional tandem MS methods. Here we describe the first application of activated ion electron transfer dissociation (AI-ETD) to proteins in the 30-70 kDa range. AI-ETD leverages infrared photo-activation concurrent to ETD reactions to improve sequence-informative product ion generation

SUBMITTER: Riley NM 

PROVIDER: S-EPMC5786479 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature