Finding the right fold

被引：70

作者：

Goldenberg, DP ^{[1
]}

机构：

[1] Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1999年 / 6卷 / 11期

关键词：

D O I：

10.1038/14866

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：

Using mutational analysis, three groups have compared the transition states for the folding of two pairs of homologous proteins. The results of these studies suggest that protein folding mechanisms are conserved and are defined primarily by the overall topology of the native structures, as opposed to specific details of the interactions stabilizing these structures.

引用

页码：987 / 990

页数：4

共 23 条

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