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3D Protein Structures by Solid‐State NMR Spectroscopy: Ready for High Resolution
Author(s) -
Böckmann Anja
Publication year - 2008
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.200801352
Subject(s) - nuclear magnetic resonance spectroscopy , solid state nuclear magnetic resonance , high resolution , spectroscopy , solid state , membrane protein , chemistry , structural biology , protein structure , crystallography , resolution (logic) , materials science , membrane , physics , nuclear magnetic resonance , computer science , stereochemistry , biochemistry , remote sensing , artificial intelligence , geology , quantum mechanics
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.