Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 732-739 |
| Number of pages | 8 |
| Journal | Chembiochem |
| Volume | 13 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 19 Mar 2012 |