REFOLDING OF BOVINE PANCREATIC TRYPSIN-INHIBITOR VIA NONNATIVE DISULFIDE INTERMEDIATES
REFOLDING OF BOVINE PANCREATIC TRYPSIN-INHIBITOR VIA NONNATIVE DISULFIDE INTERMEDIATES
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DOI：
10.1006/jmbi.1995.0309
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发表时间：
1995-06-02
影响因子：
5.6
通讯作者：
CREIGHTON, TE
中科院分区：
文献类型：
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作者：
DARBY, NJ;MORIN, PE;CREIGHTON, TE
牛胰蛋白酶抑制剂（BPTI）的二硫折叠途径，特别是在二硫阶段，已经被丝氨酸取代一个或两个特定的半胱氨酸残基解剖。这限制了可能的二硫化物种类，并且观察到的二硫化物偶联折叠动力学揭示了剩余种类的作用。结果证实了两个具有非天然第二二硫键的特定二硫中间体（30- 51,5 -14）和（30- 51,5 -38）在原始BPTI途径中的动力学作用。此外，通过这些中间体的折叠速率被证明可以定量地解释正常蛋白质的折叠速率；因此，基本上所有的分子都通过这两种特殊的中间产物重新折叠。它们是折叠途径中最多产的，它们的作用很容易根据它们的构象来解释。
The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI), especially at the two-disulphide stage, has been dissected by replacing one or two particular cysteine residues by serine. This restricts which disulphide species are possible, and the observed kinetics of disulphide-coupled folding reveal the roles of the remaining species.The results obtained confirm the kinetic roles in the original BPTI pathway of the two specific two-disulphide intermediates with non-native second disulphide bonds, (30-51, 5-14) and (30-51, 5-38). Moreover, the rates of folding through each of these intermediates are shown to account quantitatively for the rate of folding of the normal protein; therefore, essentially all the molecules refold through these two particular intermediates. They are amongst the most productive on the folding pathway, and their roles are readily explicable on the basis of their conformations.