蛋白质折叠机制。IV. 牛胰蛋白酶抑制剂中二硫键的形成与断裂

Mechanism of protein folding. IV. Forming and breaking of disulfide bonds in bovine pancreatic tripsin inhibitor.

作者信息

Kobayashi Y, Sasabe H, Akutsu T, Saitô N

机构信息

Frontier Research Program, RIKEN Institute, Saitama, Japan.

出版信息

Biophys Chem. 1992 Sep;44(2):113-27. doi: 10.1016/0301-4622(92)85043-4.

DOI:10.1016/0301-4622(92)85043-4

PMID:1382647

Abstract

The folding mechanism of bovine pancreatic tripsin inhibitor (BPTI) is explained theoretically on the basis of the island model, where the driving force of folding is hydrophobic interaction. For this purpose, we take a look at the formation and breaking of disulfide bonds during the folding process of BPTI. The intermediate conformations and the native one are successfully obtained, which satisfy the so-called "lampshade" geometrical criterion for the formation of the disulfide bonds. The folding pathway is consistent with the renaturation experiment by Creighton. In addition, an elaborate treatment of side chains of amino acid residues by the software programme CHARMm confirms quantitatively the formation of disulfide bridges.

摘要

基于岛屿模型从理论上解释了牛胰蛋白酶抑制剂（BPTI）的折叠机制，其中折叠的驱动力是疏水相互作用。为此，我们研究了BPTI折叠过程中二硫键的形成与断裂。成功获得了中间构象和天然构象，它们满足二硫键形成的所谓“灯罩”几何标准。折叠途径与Creighton的复性实验一致。此外，通过软件程序CHARMm对氨基酸残基侧链进行精细处理，定量证实了二硫桥的形成。