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Back Cover: DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells (Angew. Chem. Int. Ed. 37/2019)
Author(s) -
Narasimhan Siddarth,
Scherpe Stephan,
Lucini Paioni Alessandra,
van der Zwan Johan,
Folkers Gert E.,
Ovaa Huib,
Baldus Marc
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201908849
Subject(s) - solid state nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , spectroscopy , cover (algebra) , int , solid state , chemistry , isotopic labeling , isotope , two dimensional nuclear magnetic resonance spectroscopy , crystallography , analytical chemistry (journal) , materials science , nuclear magnetic resonance , stereochemistry , physics , organic chemistry , nuclear physics , quantum mechanics , mechanical engineering , engineering , computer science , operating system
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.