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 (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 …

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 concentration. …

A new instrument configuration for native ion mobility-mass spectrometry (IM-MS) is described.
Macromolecule ions are generated by using a static ESI source coupled to an RF ion …

Chaperonins are nanomachines that harness ATP hydrolysis to power and catalyze protein
folding, a chemical action that is directly linked to the maintenance of cell function through …

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 obtained …

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

TRAAK is an ion channel from the two-pore domain potassium (K 2P ) channel family with
roles in maintaining the resting membrane potential and fast action potential conduction. …

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 …

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). The …