Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using 19F nuclear magnetic resonance

作     者：Dong Li(1) Juan Li(1) Yonglong Zhuang(3) Longhua Zhang(1) Ying Xiong(1) Pan Shi (2) Changlin Tian (1)(2) 

作者机构：1.Hefei National Laboratory for Physical Science at the Microscale & School of Life Science University of Science and Technology of China Hefei 230026 China 3.Department of Chemistry Anhui University Hefei 230027 China 2.High Magnetic Field Laboratory Chinese Academy of Sciences Hefei 230031 China 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2015年第6卷第3期

页      面：229-233页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 0809[工学-电子科学与技术（可授工学、理学学位）] 07[理学] 070205[理学-凝聚态物理] 08[工学] 0805[工学-材料科学与工程（可授工学、理学学位）] 080502[工学-材料学] 0702[理学-物理学] 

基　　金：supported by the National Basic Research Program (973 Program) 国家自然科学基金 Strategic Priority Research Program of CAS 

主　　题：Unnatural Amino Acid Interaction Partner Protein Phosphorylation Analysis Amber Stop Codon Membrane Scaffold Protein 

摘      要：Dear Editor, Among many of biophysical methods, 19F NMR spectros- copy has emerged as a powerful tool for characterizing protein structure, dynamics and function properties due to high intrinsic sensitivities of fluorine, 100% natural abundance of the NMR-active spin, the absence of any natural background in cells, and exquisite sensitivities of 19F chemical shift to environment （Shi et al., 2011; Shi et al.,