Effi cient long-distance NMR-PRE and EPR-DEER restraints for two-domain protein structure determination  

作　　者：Kaiqi Wu Chaowei Shi Juan Li Haipeng Wang Pan Shi Liu Chen Fangming Wu Ying Xiong Changlin Tian 

机构地区：[1]Hefei National Laboratory for Physical Science at the Microscale&School of Life Science,University of Science and Technology of China,Hefei 230026,China [2]High Magnetic Field Laboratory,Chinese Academy of Sciences,Hefei 230031,China

出　　处：《Protein & Cell》2013年第12期893-896,共4页蛋白质与细胞（英文版）

基　　金：This research was supported by the National Basic Research Program(973 Program)(Nos.2011CB911104 and 2013CB910200);the Chinese Natural Science Foundation of China(Grant No.31100563)to Y.Xiong and(Grant No.31170817)to C.Tian.

摘　　要：Dear Editor,The functional diversity of proteins is related to the cooperation of multiple domains.Independent globular domains are typically joined by a fl exible length of polypeptide chain,which makes the structural analysis of multi-domain proteins diffi cult.Here,we describe the combined use of solution NMR(nuclear magnetic resonance)and EPR(elec-tron paramagnetic resonance)for the structural analysis of a protein with two separate domains.The structure of each domain was determined independently using conventional NMR restraints,and the relative orientation of the two separate domains was confi ned using long-distance restraints obtained by NMR-PRE(paramagnetic relaxation enhancement)and EPR-DEER(double electron-electron resonance,also called PELDOR:pulsed electron double reso-nance.

关 键 词：PARAMAGNETIC structure double 

分 类 号：O17[理学—数学]