The proteome, or collection of proteoforms expressed in a biological system, is dynamic and
heterogeneous. As our appreciation for the complexity of the proteome has evolved, so have …

Recent developments in ion mobility (IM) technology have expanded the capability to
separate and characterize gas-phase ions of biomolecules, especially when paired with …

“Top-down” proteomics analyzes intact proteins and identifies proteoforms by their intact
mass as well as the observed fragmentation pattern in tandem mass spectrometry (MS/MS) …

Ion activation methods carried out at gas pressures compatible with ion mobility separations
are not yet widely established. This limits the analytical utility of emerging tandem-ion …

Native ion mobility/mass spectrometry is well-poised to structurally screen proteomes but
characterizes protein structures in the absence of a solvent. This raises long-standing …

High-field asymmetric waveform ion mobility spectrometry (FAIMS) separates glycopeptides
in the gas phase prior to mass spectrometry (MS) analysis, thus offering the potential to …

Continuing advances in proteomics highlight the ubiquity and biological importance of
proteoforms─ proteins with varied sequence, splicing, or distribution of post-translational …

Mass spectrometry (MS)-based proteomics workflows of intact protein ions have increasingly
been utilized to study biological systems. These workflows, however, frequently result in …

Recent advances have rekindled the interest in ion mobility as an additional dimension of
separation in mass spectrometry (MS)-based proteomics. Ion mobility separates ions …

Enzymatic catalysis is one of the fundamental processes that drives the dynamic landscape
of post‐translational modifications (PTMs), expanding the structural and functional diversity …