PROTEIN STABILITY EFFECTS OF A COMPLETE SET OF ALANINE SUBSTITUTIONS IN ARE REPRESSOR

被引：121
|
作者：
MILLA, ME [1 ]
BROWN, BM [1 ]
SAUER, RT [1 ]
机构：
[1] MIT,DEPT BIOL,CAMBRIDGE,MA 02139
来源：
NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 08期
关键词：
D O I：
10.1038/nsb0894-518
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 equilibrium stabilities of a complete set of single alanine-substitution mutants of the Arc repressor of bacteriophage P22 have been determined by thermal and urea denaturation experiments. Only half the alanine substitutions cause significant changes in stability, with the most deleterious mutations affecting side chains in the hydrophobic core or in salt bridges and hydrogen bonds which are protected from solvent. The five mutations that are most destabilizing affect a cluster of core residues that seem to form a structural foundation for Arc.
引用
收藏
页码：518 / 523
页数：6
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