Linear correlation between thermal stability and folding kinetics of lysozyme

被引：33

作者：

Cao, A ^{[1
]}

Wang, G ^{[1
]}

Tang, YQ ^{[1
]}

Lai, LH ^{[1
]}

机构：

[1] Peking Univ, Coll Chem, State Key Lab Struct Chem Stable & Unstable Speci, Beijing 100871, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 291卷 / 04期

基金：

中国国家自然科学基金;

关键词：

protein folding; pH dependence; lysozyme; stopped-flow; circular dichroism; differential scanning calorimetry;

D O I：

10.1006/bbrc.2002.6526

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：

We have studied the refolding and thermal denaturation of hen egg white lysozyme in a wide range of pH values (from 1.5 to 9.4) using stopped-flow circular dichroism (CD) and differential scanning calorimetry (DSC). A linear correlation was found between the thermal denaturation temperature (T.) and the logarithm of the refolding rate of the slow folding phase of hen egg white lysozyme (Ink(2)). (C) 2002 Elsevier Science (USA).

引用

收藏

页码：795 / 797

页数：3

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