Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR

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	Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
	Yang, Jun 1,2,3; Aslimovska, Lubica 1,2; Glaubitz, Clemens 1,2
刊名	JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
	2011-04-06
卷号	133 期号:13 页码:4874-4881
产权排序	第三
英文摘要	Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein structure. In the current study, high-resolution solid-state NMR at high magnetic field was used to investigate their effects on the molecular dynamics of green proteorhodopsin, a bacterial light-driven proton pump. Through-space and through-bond correlation experiments were employed to identify and characterize highly mobile and motionally restricted regions of proteorhodopsin. Our data show that hydration water plays an essential role for enhancing molecular dynamics of residues in tails and interhelical loops, while it is found less important for residues in transmembrane domains or rigid, structured loop segments. In contrast, switching the lipids from the gel to their liquid crystalline phase enhances molecular fluctuations mainly in transmembrane helices on a time scale of 10 but has little effect on loop and tail residues. Increased mobility is especially observed in helices C, F, and G, but also in the EF loop. Fluctuations in those regions are relevant to structural dynamics during the photocycle of proteorhodopsin. Our data are important for the functional understanding of proteorhodopsin, but also offer an important contribution to the general understanding of site-resolved effects of water and lipid bilayets onto the dynamic properties of membrane proteins.
学科主题	化学
WOS标题词	Science & Technology ; Physical Sciences
类目[WOS]	Chemistry, Multidisciplinary
研究领域[WOS]	Chemistry
关键词[WOS]	ANGLE-SPINNING NMR ; BIOLOGICAL-MEMBRANES ; HYDRATION-WATER ; CONFORMATIONAL-CHANGE ; PROTEIN INTERACTIONS ; SECONDARY STRUCTURE ; NEUTRON-SCATTERING ; PROTON PUMP ; SCHIFF-BASE ; BACTERIORHODOPSIN
收录类别	SCI
语种	英语
WOS记录号	WOS:000289492700044
内容类型	期刊论文
源URL	[http://ir.wipm.ac.cn/handle/112942/1855]
专题	武汉物理与数学研究所_2011年以前论文发表（包括2011年）
作者单位	1.Goethe Univ Frankfurt, Inst Biophys Chem, D-60438 Frankfurt, Germany 2.Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance, D-60438 Frankfurt, Germany 3.Chinese Acad Sci, State Key Lab Magnet Resonance & Atom & Mol Phys, Wuhan Ctr Magnet Resonance, Wuhan Inst Phys & Math, Wuhan 430071, Peoples R China
推荐引用方式 GB/T 7714	Yang, Jun,Aslimovska, Lubica,Glaubitz, Clemens. Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2011,133(13):4874-4881.
APA	Yang, Jun,Aslimovska, Lubica,&Glaubitz, Clemens.(2011).Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,133(13),4874-4881.
MLA	Yang, Jun,et al."Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 133.13(2011):4874-4881.