Abstract
In native mass spectrometry sample handling and measuring conditions are optimized to retain non-covalent interactions, allowing the detailed analysis of protein-protein and protein-ligand interactions. Thereby, stoichiometry, structure and dynamics of protein complexes can be studied, also by means of additional gas-phase techniques. Coupling native mass spectrometry to X-ray free-electron lasers potentially opens new routes in protein structure analysis.
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Charlotte Uetrecht 2001–2006 Biochemiestudium (Diplom) an der Universität Potsdam. 2010 Promotion an der Universität Utrecht, Niederlande. 2011–2013 Postdoc an der Uppsala Universität, Schweden. Seit 2011 (Gast-)Wissenschaftlerin an der European XFEL GmbH in Schenefeld. Seit 2014 Nachwuchsgruppenleiterin „Dynamik viraler Strukturen“ am Heinrich-Pette-Institut (HPI), Leibniz-Institut für Experimentelle Virologie in Hamburg.
Johannes Heidemann 2008–2013 Studium Molecular Life Science (B. Sc. und M. Sc.) an der Universität zu Lübeck, Masterarbeit an der University of Toronto, Kanada. Seit 2014 Promotion am Heinrich-Pette-Institut in Hamburg.
Boris Krichel 2006–2009 Biotechnologie-Studium (B. Sc.) an der Ernst-Abbe-Hochschule (EAH), Jena, Abschlussarbeit am Leibniz-Institut für Naturstoffforschung in Jena. 2009–2010 Freiwilligendienst mit der Deutschen UNESCO-Kommission in Argentinien. 2011–2013 Studium Pharmaceutical Biotechnology (M. Sc.) an der Hochschule für angewandte Wissenschaften, Hamburg. Seit 2014 Promotion am Heinrich-Pette-Institut in Hamburg.
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Heidemann, J., Krichel, B. & Uetrecht, C. Native Massenspektrometrie für die Proteinstrukturanalytik. Biospektrum 24, 164–167 (2018). https://doi.org/10.1007/s12268-018-0907-8
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DOI: https://doi.org/10.1007/s12268-018-0907-8