Here we present a guide to ion mobility mass spectrometry experiments, which covers both
linear and nonlinear methods: what is measured, how the measurements are done, and how …

The field of ion mobility-mass spectrometry (IM-MS) has grown with significant momentum in
recent years in both fundamental advances and pioneering applications. A search of the …

In bottom-up proteomics, peptides are separated by liquid chromatography with elution peak
widths in the range of seconds, whereas mass spectra are acquired in about 100 …

Collision cross section (CCS) measurements resulting from ion mobility–mass spectrometry
(IM-MS) experiments provide a promising orthogonal dimension of structural information in …

Collision cross sections in both helium and nitrogen gases were measured directly using a
drift cell with RF ion confinement inserted within a quadrupole/ion mobility/time-of-flight …

Ion mobility-mass spectrometry measurements which describe the gas-phase scaling of
molecular size and mass are of both fundamental and pragmatic utility. Fundamentally, such …

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 …

One difficulty in using ion mobility (IM) mass spectrometry (MS) to improve the specificity of
peptide ion assignments is that IM separations are performed using a range of pressures …

The size and shape of peptide ions in the gas phase are an under-explored dimension for
mass spectrometry-based proteomics. To investigate the nature and utility of the peptide …

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