期刊
CHEMBIOCHEM
卷 16, 期 5, 页码 746-751出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201402677
关键词
indole; isotope labeling; NMR spectroscopy; protein expression; tryptophan
资金
- Austrian Science Foundation (FWF) [I844]
NMR-based investigations of large protein complexes require optimized isotopic labeling schemes. We report new methods to introduce stable isotopes into tryptophan residues; these are fine-tuned to the requirements of the particular protein NMR experiment. Selective backbone labeling was performed by using a new -ketoacid precursor as an additive in cell-based overexpression media. Additionally, we developed synthetic routes to certain isotopologues of indole with C-13-H-1 spin systems surrounded by C-12 and H-2. The corresponding proteins, overexpressed in the presence of these precursor compounds, can be effectively analyzed for conformational changes in tryptophan residues in response to external stimuli, such as interaction with other proteins or small molecules.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据