Conformations of intermediates in the folding of the pancreatic trypsin inhibitor.
Conformations of intermediates in the folding of the pancreatic trypsin inhibitor.
复制标题
胰腺胰蛋白酶抑制剂折叠中间体的构象。
DOI：
10.1016/0022-2836(87)90192-6
复制
发表时间：
1987
影响因子：
5.6
通讯作者：
M. Karplus
中科院分区：
文献类型：
--
作者：
D. States;T. Creighton;C. Dobson;M. Karplus
Intermediates in the folding pathway of the bovine pancreatic trypsin inhibitor (PTI) have been examined by1H nuclear magnetic resonance (n.m.r.). The intermediates were trapped during the reoxidation and consequent refolding of reduced PTI by alkylating free thiols; each intermediate contained different disulphide linkages. The n.m.r. spectra reveal that conformational features of the native protein are present in the intermediate containing just one of the three normal disulphide linkages (30–51). As additional normal disulphide bonds are formed, the conformation becomes more similar to that of the native protein. Introduction of additional but incorrect disulphide bonds does not lead to an increase in observable globular structure. A description of the folding process in terms of the conformations of the different intermediates is proposed. The significance of these results for the general mechanism of protein folding is outlined.
