Journal
CHEMBIOCHEM
Volume 18, Issue 15, Pages 1487-1491Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201700192
Keywords
histidine; imidazole; isotope labeling; NMR spectroscopy; protein expression
Funding
- University of Vienna
- Christian Doppler Laboratory for High-Content Structural Biology and Biotechnology, Austria
- Austrian Federal Ministry of Science, Research and Economy
- National Foundation for Research, Technology and Development
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The importance of NMR spectroscopy in unraveling the structural and dynamic properties of proteins is ever-expanding owing to progress in experimental techniques, hardware development, and novel labeling approaches. Multiple sophisticated methods of aliphatic residue labeling can be found in the literature, whereas the selective incorporation of NMR active isotopes into other amino acids still holds the potential for improvement. In order to close this methodological gap, we present a novel metabolic precursor for cell-based protein overexpression to assemble C-13/H-2 isotope patterns in the peptide backbone, as well as in side chain positions of a mechanistically distinguished histidine residue.
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