Mass spectrometry is a central technology in the life sciences, providing our most
comprehensive account of the molecular inventory of the cell. In parallel with developments …

Traditionally, mass spectrometry has been a powerful analytical method enabling the
structural analysis of small molecules, and later on peptides and proteins. With the advent of …

Here we describe a detailed protocol for both data collection and interpretation with respect
to ion mobility–mass spectrometry analysis of large protein assemblies. Ion mobility is a …

We have examined the architecture of a protein complex in the absence of bulk water. By
determining collision cross sections of assemblies of the trp RNA binding protein, TRAP, we …

The technique of ion mobility mass spectrometry (IM-MS) has become of increasing interest
for rapid analysis of the conformations adopted by biological macromolecules. It is currently …

Although nonnative protein conformations, including intermediates along the folding
pathway and kinetically trapped misfolded species that disfavor the native state, are rarely …

Over the last decade, scientific and engineering interests have been shifting from
conventional ion mobility spectrometry (IMS) to field asymmetric waveform ion mobility …

The conformations of desolvated ubiquitin ions, lifted into the gas phase by electrospray
ionization (ESI), were characterized by ion mobility spectrometry (IMS) and compared to the …

Matrix-assisted laser desorption/ionization (MALDI) coupled with ion mobility–mass
spectrometry (IM–MS) provides a rapid (μs–ms) means for the two-dimensional (2D) …

The amyloid β-protein (Aβ) is a seminal neuropathic agent in Alzheimer's disease (AD).
Recent evidence points to soluble Aβ oligomers as the probable neurotoxic species. Among …