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Solid‐State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side‐Chain Motion
Author(s) -
Schanda Paul,
Huber Matthias,
Boisbouvier Jérôme,
Meier Beat H.,
Ernst Matthias
Publication year - 2011
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.201103944
Subject(s) - asymmetry , dipole , tensor (intrinsic definition) , motion (physics) , solid state , magnetic dipole–dipole interaction , coupling (piping) , solid state nuclear magnetic resonance , state (computer science) , residual dipolar coupling , conformational isomerism , physics , chemical physics , chemistry , statistical physics , nuclear magnetic resonance , computer science , materials science , molecule , algorithm , classical mechanics , quantum mechanics , mathematics , metallurgy , pure mathematics
Nonsymmetric motion : Solid‐state NMR measurements of dipolar coupling tensors provide insight into protein dynamics. The hitherto ignored asymmetry of the dipolar coupling tensor contains valuable information about motional asymmetry, which was used in the first direct site‐resolved measurement of such tensors. Important motions such as rotamer jumps can now be directly detected in the solid state.