REPACKING PROTEIN INTERIORS

被引：19

作者：

SANDBERG, WS

TERWILLIGER, TC

机构：

[1] W. S. Sandberg and T. C. Terwilliger are, the Department of Biochemistry and Molecular Biology, The University of chicago, chicago, IL 60637

来源：

TRENDS IN BIOTECHNOLOGY | 1991年 / 9卷 / 02期

关键词：

D O I：

10.1016/0167-7799(91)90019-E

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Several goals of protein engineering may be achieved through redesign and repacking of protein interiors. The effects of interior apolar substitutions on protein stability depend strongly on the site of the substitution. One reason for this is that protein interiors have properties both of apolar liquids and of crystalline solids. Substitutions at interior sites affect the stability of a protein by changing the hydrophobicity, but each site in a protein has a characteristic energy associated with introducing packing changes, and the net stability depends on both of these factors.

引用

页码：59 / 63

页数：5

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