We employed random mutagenesis to determine the region of the initial unfolding of hyper-alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under highly alkaline conditions. This region comprises two alpha-helices and a calcium-binding loop. Stabilization of the region caused the stabilization of the entire protein at a high alkaline pH 12. The alkaline stability of this region was most effectively improved by hydrophobic interactions, followed by ionic interactions with Arg residues. The effect of mutations on the improvement was different with regard to the alkaline stability and thermostability. This indicated that different strategies were necessary to improve the alkaline stability and thermostability of the protein.

译文

我们采用随机诱变来确定高碱性敏感枯草杆菌蛋白酶ALP I的初始展开区域,该区域在高度碱性条件下整个蛋白质变性之前。该区域包括两个 α 螺旋和一个钙结合环。该区域的稳定导致整个蛋白质在高碱性pH 12下的稳定。通过疏水相互作用,其次是与Arg残基的离子相互作用,可以最有效地改善该区域的碱性稳定性。突变对改善的影响在碱性稳定性和热稳定性方面有所不同。这表明需要不同的策略来提高蛋白质的碱性稳定性和热稳定性。

+1
+2
100研值 100研值 ¥99课程
检索文献一次
下载文献一次

去下载>

成功解锁2个技能,为你点赞

《SCI写作十大必备语法》
解决你的SCI语法难题!

技能熟练度+1

视频课《玩转文献检索》
让你成为检索达人!

恭喜完成新手挑战

手机微信扫一扫,添加好友领取

免费领《Endnote文献管理工具+教程》

微信扫码, 免费领取

手机登录

获取验证码
登录