Back Cover: DNP-Supported Solid-State NMR Spectroscopy of Proteins Inside Mammalian Cells (Angew. Chem. Int. Ed. 37/2019)

Publication date

2019-09-09

Authors

Narasimhan, S.ISNI 0000000493311093
Scherpe, Stephan
Lucini Paioni, AlessandraISNI 0000000492910692
van der Zwan, JohanISNI 0000000397175095
Folkers, Gert EISNI 0000000390350786
Ovaa, Huib
Baldus, MarcISNI 0000000139673796

Editors

Advisors

Supervisors

Document Type

Article
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License

taverne

Abstract

Dynamic nuclear polarization (DNP) enhanced solid‐state NMR (ssNMR) spectroscopy enables atomic‐level structural studies of isotope labeled proteins at physiologically relevant concentrations in mammalian cells, irrespective of the tumbling rate of the protein of interest, as reported by H. Ovaa, M. Baldus, and co‐workers in their Communication on page 12969 ff. In the absence of DNP, NMR sensitivity levels are insufficient to conduct such studies.

Keywords

dynamic nuclear polarization, in-cell NMR, protein-protein interactions, solid-state NMR, ubiquitination, Taverne

Citation

Narasimhan, S, Scherpe, S, Lucini Paioni, A, van der Zwan, J, Folkers, G E, Ovaa, H & Baldus, M 2019, 'Back Cover: DNP-Supported Solid-State NMR Spectroscopy of Proteins Inside Mammalian Cells (Angew. Chem. Int. Ed. 37/2019)', Angewandte Chemie-International Edition, vol. 58, no. 37, pp. 13162. https://doi.org/10.1002/anie.201908849