Metanis Norman, Hilvert Donald
Laboratory of Organic Chemistry , ETH Zürich , 8093 Zürich , Switzerland . Email:
Chem Sci. 2015 Jan 1;6(1):322-325. doi: 10.1039/c4sc02379j. Epub 2014 Sep 23.
Although oxidative folding of disulfide-rich proteins is often sluggish, this process can be significantly enhanced by targeted replacement of cysteines with selenocysteines. In this study, we examined the effects of a selenosulfide and native nonnative diselenides on the folding rates and mechanism of bovine pancreatic trypsin inhibitor. Our results show that such sulfur-to-selenium substitutions alter the distribution of key folding intermediates and enhance their rates of interconversion in a context-dependent manner.
尽管富含二硫键的蛋白质的氧化折叠通常较为缓慢，但通过用硒代半胱氨酸靶向取代半胱氨酸，这一过程可得到显著增强。在本研究中，我们研究了硒代硫化物和天然及非天然二硒化物对牛胰蛋白酶抑制剂折叠速率和机制的影响。我们的结果表明，这种硫到硒的取代改变了关键折叠中间体的分布，并以上下文依赖的方式提高了它们的相互转化速率。
