Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 37, Pages 12969-12973Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201903246
Keywords
dynamic nuclear polarization; in-cell NMR; protein-protein interactions; solid-state NMR; ubiquitination
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Funding
- Netherlands Organisation for Scientific Research (NWO) (Netherlands' Magnetic Resonance Research School, NMARRS, a VICI grant) [022.005.029]
- Netherlands Organisation for Scientific Research (NWO) [700.26.121, 700.10.443]
- iNEXT, a Horizon 2020 program of the European Union [653706]
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Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid-state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high-sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in-cell solution-state NMR spectroscopy due to molecular size limitations.
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