Journal
CHEMBIOCHEM
Volume 13, Issue 5, Pages 732-739Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201100678
Keywords
isotope labeling; NMR spectroscopy; residue-type identification; resonance assignment; spectral overlap
Funding
- European Union
- Agence pour la Recherche sur le Cancer (France)
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Selective isotopic unlabeling of proteins can provide important residue-type information as well as reduce congestion of NMR spectra. However, metabolic scrambling often complicates the final isotope-labeling pattern. Here, an array of metabolic precursors is used to perform robust, residue-specific unlabeling of proteins. The resulting isotopic-labeling patterns are predictable and nicely complement NMR experiments that differentiate residue types. This approach has widespread applications, but it is particularly relevant for proteins that lack sequence complexity or a defined tertiary structure.
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