Complete Assignment of Heteronuclear Protein Resonances by Protonless NMR Spectroscopy

The detection of 13C is now amenable to high‐resolution NMR spectroscopy of proteins. A protocol for 13C homonuclear decoupling in multidimensional experiments correlates carbonyl, Cα, and Cβ nuclei (see picture). These techniques also allow the detection of side‐chain nuclei in exclusively heteronu...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2005-05, Vol.44 (20), p.3089-3092
Main Authors: Bermel, Wolfgang, Bertini, Ivano, Duma, Luminita, Felli, Isabella C., Emsley, Lyndon, Pierattelli, Roberta, Vasos, Paul R.
Format: Article
Language:English
Subjects:
Carbon Isotopes
carbon NMR spectroscopy
Chemical Sciences
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - methods
protein structures
proteins
Proteins - chemistry
Protons
spin-state selection
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Summary:The detection of 13C is now amenable to high‐resolution NMR spectroscopy of proteins. A protocol for 13C homonuclear decoupling in multidimensional experiments correlates carbonyl, Cα, and Cβ nuclei (see picture). These techniques also allow the detection of side‐chain nuclei in exclusively heteronuclear experiments, and thus the complete assignment of proteins.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200461794