Characterizing the top-down sequencing of protein ions prior to mobility separation in a timsTOF.

ABSTRACT: Mass spectrometry (MS)-based proteomics workflows of intact protein ions have increasingly been utilized to study biological systems. These workflows, however, frequently result in convoluted and difficult to analyze mass spectra. Ion mobility spectrometry (IMS) is a promising tool to overcome these limitations by separating ions by their mass- and size-to-charge ratios. In this work, we further characterize a newly developed method to collisionally dissociate intact protein ions in a trapped ion mobility spectrometry (TIMS) device. Dissociation occurs prior to ion mobility separation and thus, all product ions are distributed throughout the mobility dimension, enabling facile assignment of near isobaric product ions. We demonstrate that collisional activation within a TIMS device is capab

SUBMITTER: Graham KA 

PROVIDER: S-EPMC10042122 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature