Gd3+-chelated lipid accelerates solid-state NMR spectroscopy of   seven-transmembrane proteins

doi:10.1007/s10858-017-0120-y

CORC > 北京大学 > 化学与分子工程学院

	Gd3+-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins
	Liu, Chang ; Liu, Jing ; Xu, Xiaojun ; Xiang, ShengQi ; Wang, Shenlin
刊名	JOURNAL OF BIOMOLECULAR NMR
	2017
关键词	Paramagnetic relaxation enhancements Seven-transmembrane proteins Solid-state NMR Non-uniform sampling ANGLE-SPINNING NMR MEMBRANE-PROTEIN BACKBONE ASSIGNMENT AMYLOID FIBRILS SENSITIVITY BILAYERS RELAXATION RESONANCE SPECTRA MICROCRYSTALS
DOI	10.1007/s10858-017-0120-y
英文摘要	Solid-state NMR (SSNMR) is an attractive technique for studying large membrane proteins in membrane-mimetic environments. However, SSNMR experiments often suffer from low efficiency, due to the inherent low sensitivity and the long recycle delays needed to recover the magnetization. Here we demonstrate that the incorporation of a small amount of a Gd3+-chelated lipid, Gd3+-DMPE-DTPA, into proteoliposomes greatly shortens the spin-lattice relaxation time (H-1-T (1)) of lipid-reconstituted membrane proteins and accelerates the data collection. This effect has been evaluated on a 30 kDa, seven-transmembrane protein, Leptosphaeria rhodopsin. With the Gd3+-chelated lipid, we can perform 2D SSNMR experiments 3 times faster than by diamagnetic control. By combining this paramagnetic relaxation-assisted data collection with non-uniform sampling, the 3D experimental times are reduced eightfold with respect to traditional 3D experiments on diamagnetic samples. A comparison between the paramagnetic relaxation enhancement (PRE) effects of Cu2+- and Gd3+-chelated lipids indicates the much higher relaxivity of the latter. Hence, a tenfold lower concentration is needed for Gd3+-chelated lipids to achieve comparable PRE effects to Cu2+-chelated lipids. In addition, Gd3+-chelated lipids neither alter the protein structures nor induce significant line-width broadening of the protein signals. This work is expected to be beneficial for structural and dynamic studies of large membrane proteins by SSNMR.; National Natural Science Foundation of China [31470727]; Ministry of Science and Technology of the People's Republic of China [2016YFA0501203]; Beijing National Laboratory for Molecular Sciences; Peking University; 1000 plan for young talent program of China; SCI(E); ARTICLE; 3; 203-214; 68
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/472295]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	Liu, Chang,Liu, Jing,Xu, Xiaojun,et al. Gd3+-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins[J]. JOURNAL OF BIOMOLECULAR NMR,2017.
APA	Liu, Chang,Liu, Jing,Xu, Xiaojun,Xiang, ShengQi,&Wang, Shenlin.(2017).Gd3+-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins.JOURNAL OF BIOMOLECULAR NMR.
MLA	Liu, Chang,et al."Gd3+-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins".JOURNAL OF BIOMOLECULAR NMR (2017).