波谱学杂志2018，Vol.35Issue(1)：1-7,7.DOI:10.11938/cjmr20172575
GB1与金属离子相互作用的NMR研究
Interaction of GB1 with Metal Ions Studied by NMR Spectroscopy
摘要
Abstract
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 GB 1 weakly bound with paramagnetic lanthanide ions and paramagnetic divalent ions,including Cu2+,Mn2+ and Co2+.In contrast,GB1 did not bind with diamagnetic divalent ions,such as Ca2+,Mg2+ and Zn2+.Furthermore,it was demonstrated that there were two binding sites for Cu2+ in GB 1,but only one for lanthanide ions and divalent ions Mn2+ and Co2+.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 GB 1 as the model protein.关键词
GB1/金属离子/特异性相互作用/解离常数/结合位点Key words
GB1/metal ion/specific interaction/dissociation constant/binding site分类
数理科学引用本文复制引用
成凯,姚陈叠,徐国华,李从刚..GB1与金属离子相互作用的NMR研究[J].波谱学杂志,2018,35(1):1-7,7.基金项目
The national natural science foundation of China (21575156,21505152). （21575156,21505152）
