title: The diverse and expanding role of mass spectrometry in structural and molecular biology.
abstract: The emergence of proteomics has led to major technological advances in mass spectrometry (MS). These advancements not only benefitted MS-based high-throughput proteomics but also increased the impact of mass spectrometry on the field of structural and molecular biology. Here, we review how state-of-the-art MS methods, including native MS, top-down protein sequencing, cross-linking-MS, and hydrogen-deuterium exchange-MS, nowadays enable the characterization of biomolecular structures, functions, and interactions. In particular, we focus on the role of mass spectrometry in integrated structural and molecular biology investigations of biological macromolecular complexes and cellular machineries, highlighting work on CRISPR-Cas systems and eukaryotic transcription complexes.
authors: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Utrecht, The Netherlands.|Netherlands Proteomics Center, Utrecht, The Netherlands.
authors: Philip
authors: P
authors: Lössl
authors: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Utrecht, The Netherlands.|Netherlands Proteomics Center, Utrecht, The Netherlands.
authors: Michiel
authors: M
authors: van de Waterbeemd
authors: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Utrecht, The Netherlands a.j.r.heck@uu.nl.|Netherlands Proteomics Center, Utrecht, The Netherlands.
authors: Albert Jr
authors: AJ
authors: Heck
mesh_terms: D046911:Macromolecular Substances / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D008967:Molecular Biology / Q000639:trends*
chemical_list: D046911:Macromolecular Substances
keywords: CRISPR–Cas; RNA polymerase; ligand binding; post‐translational modifications; protein complexes