Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding

Ligand binding and unfolding of tryptophan synthase revealed by ion mobility-tandem mass spectrometry employing collision and surface induced dissociation

Understanding protein tertiary and quaternary structures is crucial to a better understanding of their biological functions. Here we illustrate for tryptophan synthase that tandem mass spectrometry (MS/MS) reveals not only protein subunit architectures, but also protein unfolding behavior when coupled with ion mobility (IM). In the present study, we verified the subunit arrangement with surface...

Ion Mobility Mass Spectrometry

for more complex analysers for automated sample processing and plant control. The separation time will continue to decrease; in the past there has been limited interest in fast separations but this could change as automated sample processing is developed. Increasing use of coupled techniques such as GC-GC, liquid chromatography-GC, and supercritical Suid chromatography-GC for the separation of ...

Ion Mobility-Mass Spectrometry

A novel approach to collision-induced dissociation (CID) for ion mobility-mass spectrometry experiments.

Collision induced dissociation (CID) combined with matrix assisted laser desorption ionization-ion mobility-mass spectrometry (MALDI-IM-MS) is described. In this approach, peptide ions are separated on the basis of mobility in a 15 cm drift cell. Following mobility separation, the ions exit the drift cell and enter a 5 cm vacuum interface with a high field region (up to 1000 V/cm) to undergo co...

Development of atmospheric pressure ionization ion mobility spectrometry and ion mobility spectrometry mass spectrometry