Abstract
Native mass spectrometry (MS) enables the characterization of macromolecular assemblies with high sensitivity. It can reveal the stoichiometry of subunits as well as their two-dimensional interaction network and provide information regarding the dynamic behavior of macromolecular complexes. Here, we describe the workflow to perform native MS experiments. In addition, we illustrate the quality control analysis of proteins using MS in denaturing conditions.
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Acknowledgment
We thank Paul Sauer, Jennifer Timm and Daniel Panne for providing the yeast CAF1 complex. We thank the members of the Viral Infection and Cancer Group at the IBS for the helpful discussion. This work used the mass spectrometry platform of the Grenoble Instruct Centre (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI (ANR-10-INSB-05-02) and GRAL (ANR-10-LABX-49-01) within the Grenoble Partnership for Structural Biology (PSB). It was financially supported by the French Infrastructure for Integrated Structural Biology Initiative and by the French National Centre for Scientific Research (CNRS).
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Boeri Erba, E., Signor, L., Oliva, M.F., Hans, F., Petosa, C. (2018). Characterizing Intact Macromolecular Complexes Using Native Mass Spectrometry. In: Marsh, J. (eds) Protein Complex Assembly. Methods in Molecular Biology, vol 1764. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7759-8_9
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DOI: https://doi.org/10.1007/978-1-4939-7759-8_9
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