Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable.
Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable.
复制标题
消除泛素的表面电荷相互作用使蛋白质折叠且非常稳定。
DOI：
10.1110/ps.29902
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发表时间：
2002
期刊：
影响因子：
--
通讯作者：
Makhatadze,GeorgeI
中科院分区：
文献类型：
--
作者：
Loladze,VakhtangV;Makhatadze,GeorgeI
使用泛素作为模型蛋白质评估了溶剂暴露的带电残基对蛋白质稳定性的贡献。我们结合定点诱变和特定化学修饰，首先用赖氨酸替换所有精氨酸残基，然后对赖氨酸氨基进行羧基化。在所有羧基均质子化的条件下（pH 2），化学修饰的蛋白质会折叠且非常稳定（ΔG = 18 kJ/mol）。这些结果表明表面电荷-电荷相互作用并不是蛋白质折叠和稳定性的重要基本力。
The contribution of solvent‐exposed charged residues to protein stability was evaluated using ubiquitin as a model protein. We combined site‐directed mutagenesis and specific chemical modifications to first replace all Arg residues with Lys, followed by carbomylation of Lys‐amino groups. Under the conditions in which all carboxylic groups are protonated (at pH 2), the chemically modified protein is folded and very stable (ΔG = 18 kJ/mol). These results indicate that surface charge–charge interactions are not an essential fundamental force for protein folding and stability.