interactionofgb1withmetalionsstudiedbynmrspectroscopy
文献类型：期刊论文
| 作者 | Cheng Kai; Yao Chendie; Xu Guohua; Li Conggang |
| 刊名 | 波谱学杂志
 |
| 出版日期 | 2018 |
| 卷号 | 35期号:1页码:1 |
| ISSN号 | 1000-4556 |
| 英文摘要 | B1 domain of staphylococcal protein G (GB1) is a widely used model protein for developing in vivo and in vitro protein structural determination methods based on paramagnetic nuclear magnetic resonance (NMR) such as pseudocontact chemical shift (PCS) and paramagnetic relaxation enhancement (PRE). However, few previous studies have investigated the interactions between GB1 and metal ions, especially paramagnetic ions. In this study, the interactions between GB1 and divalent/lanthanide metal ions were studied by NMR spectroscopy. It was found that GB1 weakly bound with paramagnetic lanthanide ions and paramagnetic divalent ions, including Cu~(2+), Mn~(2+) and Co~(2+). In contrast, GB1 did not bind with diamagnetic divalent ions, such as Ca~(2+), Mg~(2+) and Zn~(2+). Furthermore, it was demonstrated that there were two binding sites for Cu~(2+) in GB1, but only one for lanthanide ions and divalent ions Mn~(2+) and Co~(2+). The current study demonstrated that NMR spectroscopy is a powerful tool to study weak binding between protein and metal ions. And the results indicated that care must be taken to avoid possible interference to paramagnetic NMR data when using GB1 as the model protein. |
| 语种 | 英语 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/15620]  |
| 专题 | 中国科学院武汉物理与数学研究所 |
| 作者单位 | 中国科学院武汉物理与数学研究所 |
| 推荐引用方式 GB/T 7714 | Cheng Kai,Yao Chendie,Xu Guohua,et al. interactionofgb1withmetalionsstudiedbynmrspectroscopy[J]. 波谱学杂志,2018,35(1):1. |
| APA | Cheng Kai,Yao Chendie,Xu Guohua,&Li Conggang.(2018).interactionofgb1withmetalionsstudiedbynmrspectroscopy.波谱学杂志,35(1),1. |
| MLA | Cheng Kai,et al."interactionofgb1withmetalionsstudiedbynmrspectroscopy".波谱学杂志 35.1(2018):1. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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