FOLDING OF BETA-SHEET PROTEINS

被引：47

作者：

CARLSSON, U ^{[1
]}

JONSSON, BH ^{[1
]}

机构：

[1] UMEA UNIV,DEPT BIOCHEM,S-90187 UMEA,SWEDEN

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1995年 / 5卷 / 04期

关键词：

D O I：

10.1016/0959-440X(95)80032-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

In the past year, interesting new information concerning various aspects of the folding process of beta-sheet proteins has been gleaned. Kinetic and equilibrium folding intermediates have been characterized. Studies of extensively denatured states and of model peptide fragments have enabled important steps to be taken towards an understanding of the initiation of the folding process of beta-sheet proteins. Site-directed mutagenesis has been used in combination with various probes to monitor folding events.

引用

收藏

页码：482 / 487

页数：6

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