NMR studies on binding sites and aggregation-disassociation of fluorinated surfactant sodium perfluorooctanoate on protein ubiquitin
- 影响因子：
0.0
- 发表刊物：
Biochim. Biophys. Acta
- 摘要：
The fluorinated surfactant sodium perfluorooctanoate (SPFO) could bind onto ubiquitin (UBQ) and induce the unfolding of UBQ. By using (15)N-edited heteronuclear single-quantum coherence (HSQC) NMR and (19)F NMR to monitor (15)N-labeled UBQ and SPFO, respectively, the binding sites and the aggregation process of SPFO on UBQ at various SPFO concentrations were observed. A detailed process from specific binding to cooperative binding of SPFO on UBQ, and a detailed structure change of UBQ upon the increase of SPFO concentration were obtained. The refolding of UBQ in UBQ-SPFO complex was carried out by adding cationic surfactant. It was shown that added cationic surfactants formed mixed micelles with SPFO and resulted in the dissociation of the UBQ-SPFO complex, and consequently, most ubiquitin could be refolded to its native state.
- 论文类型：
期刊论文
- 论文编号：
23
- 卷号：
1790
- 期号：
2
- 页面范围：
134-140
- 是否译文：
否
- 发表时间：
2009-02-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Lu Renchao
- 通讯作者：
Xiao Jinxin
- 全部作者：
Guo Xianrong,Jin Changwen
