Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 57, Issue 22, Pages 6390-6396Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201709559
Keywords
cross-linking; mass spectrometry; protein structures; protein conformations; protein-protein interactions
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [Si 867/15-2]
- region of Saxony-Anhalt
- EU (COST Action) [BM1403]
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Structural mass spectrometry (MS) is gaining increasing importance for deriving valuable three-dimensional structural information on proteins and protein complexes, and it complements existing techniques, such as NMR spectroscopy and X-ray crystallography. Structural MS unites different MS-based techniques, such as hydrogen/deuterium exchange, native MS, ion-mobility MS, protein footprinting, and chemical cross-linking/MS, and it allows fundamental questions in structural biology to be addressed. In this Minireview, I will focus on the cross-linking/MS strategy. This method not only delivers tertiary structural information on proteins, but is also increasingly being used to decipher protein interaction networks, both in vitro and in vivo. Cross-linking/MS is currently one of the most promising MS-based approaches to derive structural information on very large and transient protein assemblies and intrinsically disordered proteins.
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