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Highly Selective Stable Isotope Labeling of Histidine Residues by Using a Novel Precursor in E. coli ‐Based Overexpression Systems
Author(s) -
Schörghuber Julia,
Geist Leonhard,
Platzer Gerald,
Konrat Robert,
Lichtenecker Roman J.
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700192
Subject(s) - histidine , chemistry , isotopic labeling , combinatorial chemistry , isotope , escherichia coli , stable isotope ratio , biochemistry , stereochemistry , organic chemistry , gene , amino acid , physics , quantum mechanics
Abstract 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 13 C/ 2 H isotope patterns in the peptide backbone, as well as in side chain positions of a mechanistically distinguished histidine residue.