Schörghuber Julia, Geist Leonhard, Platzer Gerald, Konrat Robert, Lichtenecker Roman J
Institute of Organic Chemistry, University of Vienna, Währingerstrasse 38, 1090, Vienna, Austria.
Christian Doppler Laboratory for High-Content Structural Biology, and Biotechnology/Department of Structural and Computational Biology, University of Vienna, 1090, Vienna, Austria.
Chembiochem. 2017 Aug 4;18(15):1487-1491. doi: 10.1002/cbic.201700192. Epub 2017 Jun 12.
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/ H isotope patterns in the peptide backbone, as well as in side chain positions of a mechanistically distinguished histidine residue.
由于实验技术、硬件开发和新型标记方法的进步,核磁共振光谱在揭示蛋白质的结构和动态特性方面的重要性正在不断扩大。文献中可以找到多种复杂的脂肪族残基标记方法,而将核磁共振活性同位素选择性地掺入其他氨基酸仍有改进的潜力。为了弥补这一方法上的差距,我们提出了一种用于基于细胞的蛋白质过表达的新型代谢前体,以在肽主链以及一个具有独特机制的组氨酸残基的侧链位置组装碳/氢同位素模式。