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Complete Assignment of Heteronuclear Protein Resonances by Protonless NMR Spectroscopy
Author(s) -
Bermel Wolfgang,
Bertini Ivano,
Duma Luminita,
Felli Isabella C.,
Emsley Lyndon,
Pierattelli Roberta,
Vasos Paul R.
Publication year - 2005
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.200461794
Subject(s) - homonuclear molecule , heteronuclear molecule , nuclear magnetic resonance spectroscopy , decoupling (probability) , chemistry , spectroscopy , transverse relaxation optimized spectroscopy , heteronuclear single quantum coherence spectroscopy , high resolution , nuclear magnetic resonance , physics , fluorine 19 nmr , molecule , organic chemistry , engineering , quantum mechanics , remote sensing , control engineering , geology
The detection of 13 C is now amenable to high‐resolution NMR spectroscopy of proteins. A protocol for 13 C homonuclear decoupling in multidimensional experiments correlates carbonyl, C α , and C β nuclei (see picture). These techniques also allow the detection of side‐chain nuclei in exclusively heteronuclear experiments, and thus the complete assignment of proteins.