¹⁹F NMR 化学位移及侧链弛豫分析标记非天然氨基酸的膜蛋白的位点特异性。
Site-specific ¹⁹F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
机构信息
National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
出版信息
Protein Sci. 2011 Jan;20(1):224-8. doi: 10.1002/pro.545.
Abstract
Site-specific ¹⁹F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one-dimensional ¹⁹F spectra and T₁, T₂ relaxation data were acquired on a SH3 domain in aqueous buffer containing 60% glycerol, and a nine-transmembrane helices membrane protein diacyl-glycerol kinase (DAGK) in dodecyl phosphochoine (DPC) micelles. The high quality of the data indicates that this method can be applied to site-specifically analyze side chain internal mobility of membrane proteins or large size proteins.
摘要
¹⁹F 化学位移和侧链弛豫分析可应用于大型蛋白质。在此，在含有 60%甘油的水溶液缓冲液中对 SH3 结构域以及十二烷基磷酸胆碱（DPC）胶束中的九跨膜螺旋膜蛋白二酰基甘油激酶（DAGK）进行一维 ¹⁹F 谱和 T₁、T₂弛豫数据采集。高质量的数据表明，该方法可用于对膜蛋白或大型蛋白质的侧链内部流动性进行特异性分析。
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