Abstract
Recent development of ion mobility mass spectrometry (IM-MS) with electrospray ionization (ESI) has enabled the characterization of protein assemblies which play important roles in various events in living cells. Some proteins change their conformations by target recognition. Therefore, the conformational analysis with a small amount of proteins is helpful to understand the mechanism of biological events. By IM-MS, proteins with the same masses but different conformations can be separated, and the information on the shape of analyte ions can be obtained even for the protein assemblies. In this article, an overview of traveling-wave IM-MS for biomolecules is described, showing an example of IM-MS for a globular protein, bovine Ubiquitin. In addition, application of IM-MS to characterize the structure of an intrinsically disordered protein complex, Swi5-Sfr1, is demonstrated.
