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 …

Ion mobility spectrometry/mass spectrometry (IMS/MS) is widely used to study various levels
of protein structure. Here, we review the current state of affairs in tandem-trapped ion …

Post-translational modifications (PTMs) on intact histones play a major role in regulating
chromatin dynamics and influence biological processes such as DNA transcription …

Trapped ion mobility spectrometry (TIMS) when coupled with mass spectrometry (MS) offers
great advantages for the separation of isobaric, isomeric, and/or conformeric species. In the …

“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 …

Ion mobility mass spectrometry (IM-MS) has proven to be an excellent method to
characterize the structure of amyloidogenic protein and peptide aggregates, which are …

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

Carbohydrates play important roles in biological processes, but their identification remains a
significant analytical problem. While mass spectrometry has increasingly enabled the …

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