This work has been supported by the French ANR (JC05_44957, ANR-07-PCVI-0013-03). I thank Antoine Loquet for color figures.
3D Protein Structures by Solid-State NMR Spectroscopy: Ready for High Resolution†
Article first published online: 4 JUL 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 47, Issue 33, pages 6110–6113, August 4, 2008
How to Cite
Böckmann, A. (2008), 3D Protein Structures by Solid-State NMR Spectroscopy: Ready for High Resolution. Angew. Chem. Int. Ed., 47: 6110–6113. doi: 10.1002/anie.200801352
- Issue published online: 29 JUL 2008
- Article first published online: 4 JUL 2008
- French ANR. Grant Numbers: JC05_44957, ANR-07-PCVI-0013-03
- membrane proteins;
- NMR spectroscopy;
- protein structures
Protocols for determining high-resolution 3D structures of solid proteins are essential for structural studies of fibrils and membrane proteins. Advances in solid-state NMR spectroscopy have led to a multitude of approaches to access restraints and to calculate structures from highly ambiguous data sets. 3D structures at atomic resolution have been derived for several model proteins, as well as for the C-terminal portion of the Het-s prion protein.