PROTEIN STABILIZATION BY HYDROPHOBIC INTERACTIONS AT THE SURFACE

被引：1
|
作者：
VANDENBURG, B
DIJKSTRA, BW
VRIEND, G
VANDERVINNE, B
VENEMA, G
EIJSINK, VGH
机构：
[1] RUG, CTR BIOL SCI, DEPT GENET, 9751 NN HAREN, NETHERLANDS
[2] UNIV GRONINGEN, BIOSON RES INST, GRONINGEN, NETHERLANDS
[3] EMBL, PROT DESIGN GRP, HEIDELBERG, GERMANY
来源：
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 220卷 / 03期
关键词：
D O I：
暂无
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：
The contribution of the solvent-exposed residue 63 to thermal stability of the thermolysin-like neutral protease of Bacillus stearothermophilus was studied by analyzing the effect of twelve different amino acid substitutions at this position. The thermal stability of the enzyme was increased considerably by introducing Arg, Lys or bulky hydrophobic amino acids. In general, the effects of the mutations showed that hydrophobic contacts in this surface-located region of the protein are a major determinant of thermal stability. This observation contrasts with general concepts concerning the contribution of surface-located residues and surface hydrophobicity to protein stability and indicates new ways for protein stabilization by site-directed mutagenesis.
引用
收藏
页码：981 / 985
页数：5
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