UNDERSTANDING HOW PROTEINS FOLD - THE LYSOZYME STORY SO FAR

被引：329

作者：

DOBSON, CM

EVANS, PA

RADFORD, SE

机构：

[1] UNIV OXFORD,NEW CHEM LAB,OXFORD OX1 3QT,ENGLAND

[2] UNIV CAMBRIDGE,CAMBRIDGE CTR MOLEC RECOGNIT,CAMBRIDGE CB2 1QW,ENGLAND

[3] UNIV CAMBRIDGE,DEPT BIOCHEM,CAMBRIDGE CB2 1QW,ENGLAND

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1994年 / 19卷 / 01期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0968-0004(94)90171-6

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：

Hen lysozyme is one of the best characterized and most studied of all proteins. Recently, we have used a range of different methods to examine the events involved in the in vitro folding pathway of this protein. In this review we show that, by combining complementary techniques, it has been possible to piece together a detailed model for the folding of this enzyme. Important questions prompted by this work are highlighted and we then propose some ideas consistent with our data, as well as those of others, which we believe begin to provide insight into one of the most intriguing of structural problems in biology - how proteins can achieve their complex native forms from disordered denatured states.

引用

页码：31 / 37

页数：7

共 39 条

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