Native mass spectrometry (MS) is aimed at preserving and determining the native structure,
composition, and stoichiometry of biomolecules and their complexes from solution after they …

The structures and conformational dynamics of proteins, protein complexes, and their
noncovalent interactions with other molecules are controlled specifically by the Gibbs free …

Stabilities and structure (s) of proteins are directly coupled to their local environment or
Gibbs free energy landscape as defined by solvent, temperature, pressure, and …

Transthyretin (TTR) is a tetrameric protein transporting hormones in the plasma and brain,
which has many other activities that have not been fully acknowledged. TTR is a positive …

Studies of large proteins, protein complexes, and membrane protein complexes pose new
challenges, most notably the need for increased ion mobility (IM) and mass spectrometry …

Rotationally averaged collision cross section (CCS) values for a series of proteins and
protein complexes ranging in size from 8.6 to 810 kDa are reported. The CCSs were …

Iron–sulfur (Fe–S) clusters are ubiquitous protein cofactors that are required for many
important biological processes including oxidative respiration, nitrogen fixation, and …

Here, we describe a digital-waveform dual-quadrupole mass spectrometer that enhances
the performance of our drift tube FT-IMS high-resolution Orbitrap mass spectrometer (MS) …

Native ion mobility-mass spectrometry (IM-MS) is an emerging biophysical approach to
probe the intricate details of protein structure and function. The instrument design enables …

There is growing interest in the characterization of protein complexes and their interactions
with ligands using native ion mobility mass spectrometry. A particular challenge, especially …