Structural identification of electron transfer dissociation products in mass spectrometry using infrared ion spectroscopy.

ABSTRACT: Tandem mass spectrometry occupies a principle place among modern analytical methods and drives many developments in the 'omics' sciences. Electron attachment induced dissociation methods, as alternatives for collision-induced dissociation have profoundly influenced the field of proteomics, enabling among others the top-down sequencing of entire proteins and the analysis of post-translational modifications. The technique, however, produces more complex mass spectra and its radical-driven reaction mechanisms remain incompletely understood. Here we demonstrate the facile structural characterization of electron transfer dissociation generated peptide fragments by infrared ion spectroscopy using the tunable free-electron laser FELIX, aiding the elucidation of the underlying dissociation mechani

SUBMITTER: Martens J 

PROVIDER: S-EPMC4906228 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature