interactionofgb1withmetalionsstudiedbynmrspectroscopy

	interactionofgb1withmetalionsstudiedbynmrspectroscopy
	Cheng Kai; Yao Chendie; Xu Guohua; Li Conggang
刊名	波谱学杂志
	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
内容类型	期刊论文
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.