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.
Original language | English |
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Pages (from-to) | 13162 |
Number of pages | 1 |
Journal | Angewandte Chemie-International Edition |
Volume | 58 |
Issue number | 37 |
DOIs | |
Publication status | Published - 9 Sept 2019 |
Keywords
- dynamic nuclear polarization
- in-cell NMR
- protein-protein interactions
- solid-state NMR
- ubiquitination