Keeping it in the family: folding studies of related proteins

被引：103

作者：

Gunasekaran, K ^{[1
]}

Eyles, SJ

Hagler, AT

Gierasch, LM

机构：

[1] Univ Massachusetts, Dept Biochem & Mol Biol, Amherst, MA 01003 USA

[2] Univ Massachusetts, Dept Chem, Amherst, MA 01003 USA

[3] Univ Massachusetts, Dept Polymer Sci & Engn, Amherst, MA 01003 USA

[4] Struct Proteom, San Diego, CA USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2001年 / 11卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(00)00173-1

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：

Investigators have recently turned to studies of protein families to shed light on the mechanism of protein folding. In small proteins for which detailed analysis has been performed, recent studies show that transition-state structure is generally conserved. The number and structures of populated folding intermediates have been found to vary in homologous families of larger (greater than 100-residue) proteins, reflecting a balance of local and global interactions.

引用

页码：83 / 93

页数：11

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