Circular dichroism of denatured barstar suggests residual structure

被引：35
作者：
Nolting, B
Golbik, R
SolerGonzalez, AS
Fersht, AR
机构：
[1] UNIV CAMBRIDGE, CHEM LAB, CAMBRIDGE CB2 2QH, ENGLAND
[2] MRC CTR, CAMBRIDGE CTR PROT ENGN, CAMBRIDGE CB2 2QH, ENGLAND
来源：
BIOCHEMISTRY | 1997年 / 36卷 / 32期
关键词：
D O I：
10.1021/bi962879u
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 circular dichroism (CD) spectrum of the denatured state of barstar has been analyzed as a function of urea and temperature. The near-and far-UV CD spectra change very rapidly in magnitude and shape with increasing temperature, unlike those of native protein, suggesting the presence of residual structure that changes with denaturing conditions. The effect of mutations indicates that there is residual. structure in helix(1) of the protein, consistent with NMR data. The changes in CD with conditions are consistent with the denatured state being a mixture of conformations of similar energy.
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收藏
页码：9899 / 9905
页数：7
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