期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 140, 期 5, 页码 1568-1571出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b10230
关键词
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资金
- EU [675071]
- Croucher Foundation Fellowship
- Biotechnology and Biological Sciences Research Council [BB/J014346/1, BB/P026311/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1658062] Funding Source: researchfish
- BBSRC [BB/J014346/1] Funding Source: UKRI
The incorporation of fluorine can not only significantly facilitate the study of proteins but also potentially modulate their function. Though some biosynthetic methods allow global residue-replacement, post-translational fluorine incorporation would constitute a fast and efficient alternative. Here, we reveal a mild method for direct protein radical trifluoromethylation at native residues as a strategy for symmetric-multifluorine incorporation on mg scales with high recoveries. High selectivity toward tryptophan residues enhanced the utility of this direct trifluoromethylation technique allowing ready study of fluorinated protein constructs using F-19-NMR.
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