KINETIC ROLES AND CONFORMATIONAL PROPERTIES OF THE NONNATIVE 2-DISULFIDE INTERMEDIATES IN THE REFOLDING OF BOVINE PANCREATIC TRYPSIN-INHIBITOR

被引：31

作者：

DARBY, NJ ^{[1
]}

VANMIERLO, CPM ^{[1
]}

SCOTT, GHE ^{[1
]}

NEUHAUS, D ^{[1
]}

CREIGHTON, TE ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,W-6900 HEIDELBERG,GERMANY

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 224卷 / 04期

关键词：

PROTEIN FOLDING; DISULFIDE BONDS; BOVINE PANCREATIC TRYPSIN INHIBITOR; NUCLEAR MAGNETIC RESONANCE;

D O I：

10.1016/0022-2836(92)90458-V

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 most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule. © 1992.

引用

页码：905 / 911

页数：7

共 22 条

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[2]

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