Structural reorganization renders enhanced metalloprotein stability

被引:1
作者
Botelho, Hugo M. [1 ]
Gomes, Claudio M. [1 ]
机构
[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, EAN, P-2785572 Oeiras, Portugal
关键词
DESULFOVIBRIO-GIGAS RUBREDOXIN; CLOSTRIDIUM-PASTEURIANUM; MESOPHILIC RUBREDOXIN; CIRCULAR-DICHROISM; NMR STRUCTURE; PROTEINS; RESOLUTION; DYNAMICS; MODEL;
D O I
10.1039/c1cc13354c
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural inter-conversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.
引用
收藏
页码:11149 / 11151
页数:3
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