MECHANISM OF PROTEIN FOLDING .4. FORMING AND BREAKING OF DISULFIDE BONDS IN BOVINE PANCREATIC TRIPSIN INHIBITOR

被引：18

作者：

KOBAYASHI, Y ^{[1
]}

SASABE, H ^{[1
]}

AKUTSU, T ^{[1
]}

SAITO, N ^{[1
]}

机构：

[1] WASEDA UNIV, DEPT APPL PHYS, SHINJU KU, TOKYO 169, JAPAN

来源：

BIOPHYSICAL CHEMISTRY | 1992年 / 44卷 / 02期

关键词：

BOVINE PANCREATIC TRIPSIN INHIBITOR; CREIGHTON RENATURATION EXPERIMENT; DISULFIDE BOND; INTERMEDIATE STATE; ISLAND MODEL;

D O I：

10.1016/0301-4622(92)85043-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：113 / 127

页数：15

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