Native mass spectrometry—A valuable tool in structural biology
Marie Barth, Carla Schmidt
Abstract
Improvements in instrumentation and technology further advanced the application of MS and enabled the development of numerous specialised techniques. One such technique is ‘native’ MS, which is the analysis of intact proteins and protein complexes in the gas phase of a mass spectrometer. During native MS, non-covalent interactions between proteins and their ligands, e.g. other proteins, nucleotides, lipids or other small molecules, are maintained. The obtained mass spectra therefore reveal the composition and stoichiometry of the formed complexes. Native MS further provides information on subunit interactions and topology as well as heterogeneity of the assemblies. Native MS, consequently, takes an important role in the structural analysis of proteins and protein complexes by MS. In this tutorial, Marie Barth and Carla Schmidt introduce the application of native MS, including sample preparation, instrument requirements and data analysis, and discuss advanced applications such as ion mobility (IM) and high-resolution native MS. Carla Schmidt is professor at the Institute for Biochemistry and Biotechnology of the Martin Luther University Halle-Wittenberg (Halle, Germany). Her work focuses on the structure of membrane proteins and their interactions with the surrounding membrane with a special emphasis on the analysis of synaptic protein complexes in the context of neurodegenerative disease.