The investigation of macromolecular biomolecules with ion mobility mass spectrometry (IM-
MS) techniques has provided substantial insights into the field of structural biology over the …

Mass spectrometry-based biomolecular analyses have become permanent fixtures of
academic, industrial, and clinical research settings. The rise in utilization of mass …

Post-translational modifications (PTMs) create vast structural and functional diversity of
proteins, ultimately modulating protein function and degradation, influencing cellular …

Progress in structural biology research has led to a high demand for powerful and yet
complementary analytical tools for structural characterization of proteins and protein …

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 …

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

Protein glycosylation is one of the most common posttranslational modifications, and plays
an essential role in a wide range of biological processes such as immune response …

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 …

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 …

Unambiguous identification of distinct proteoforms and their biological functions is a
significant analytical challenge due to the many combinations of post-translational …