Apomyoglobin stability as dependent on urea concentration and temperature at two pH values

被引：7

作者：

Baryshnikova, EN ^{[1
]}

Sharapov, MG ^{[1
]}

Kashparov, IA ^{[1
]}

Ilyina, NB ^{[1
]}

Bychkova, VE ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia

来源：

MOLECULAR BIOLOGY | 2005年 / 39卷 / 02期

关键词：

apomyoglobin; stability; cooperation; urea unfolding;

D O I：

10.1007/s11008-005-0041-9

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：

Equilibrium unfolding of apomyoglobin (ApoMb) in the presence of urea was studied as dependent on the temperature (5-25 degrees C) at two pH values (5.7 and 6.2). Thermodynamic parameters of ApoMb transition from the native to the unfolded state were estimated under various conditions. Conformational changes in ApoMb were detected by tryptophan fluorescence and far-UV circular dichroism. The ApoMb stability and the cooperativity of its unfolding at 5 degrees C were considerably lower than at other temperatures at both pH values, where ApoMb is in the native conformation.

引用

页码：292 / 297

页数：6

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