CONFORMATIONAL STABILITY OF GLOBULAR-PROTEINS

被引：385
|
作者：
PACE, CN
机构：
[1] Biochemistry Department, Texas A and M University, College Station
来源：
TRENDS IN BIOCHEMICAL SCIENCES | 1990年 / 15卷 / 01期
关键词：
D O I：
10.1016/0968-0004(90)90124-T
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 conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins. © 1990.
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页码：14 / 17
页数：4
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