Solid-State NMR Shows That Dynamically Different Domains of Membrane Proteins Have Different Hydration Dependence
文献类型：期刊论文
| 作者 | Zhang, Zhengfeng; Chen, Yanke; Tang, Xinqi; Li, Jianping; Wang, Liying; Yang, Jun |
| 刊名 | JOURNAL OF PHYSICAL CHEMISTRY B
 |
| 出版日期 | 2014-08-14 |
| 卷号 | 118期号:32页码:9553-9564 |
| 英文摘要 | Hydration has a profound influence on the structure, dynamics, and functions of membrane and membrane-embedded proteins. So far the hydration response of molecular dynamics of membrane proteins in lipid bilayers is poorly understood. Here, we reveal different hydration dependence of the dynamics in dynamically different domains of membrane proteins by multidimensional magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy using 121-residue integral diacylglycerol kinase (DAGK) in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/1,2-dimyristoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (DMPG) lipid bilayers as a model system. The highly mobile and immobile domains of DAGK and their water accessibilities are identified site-specifically by scalar- and dipolar-coupling based MAS ssNMR experiments, respectively. Our experiments reveal different hydration dependence of the dynamics in highly mobile and immobile domains of membrane proteins. We demonstrate that the fast, large-amplitude motions in highly mobile domains are not triggered until 20% hydration, enhanced at 20-50% hydration and unchanged at above 50% hydration. In contrast, motions on submicrosecond time scale of immobile residues are observed to be independent of the hydration levels in gel phase of lipids, and at the temperature near gel liquid crystalline phase transition, amplitude of whole-molecule rotations around the bilayer normal is dominated by the fluidity of lipid bilayers, which is strongly hydration dependent. The hydration dependence of the dynamics of DAGK revealed by this study provides new insights into the correlations of hydration to dynamics and function of membrane proteins in lipid bilayers. |
| WOS标题词 | Science & Technology ; Physical Sciences |
| 类目[WOS] | Chemistry, Physical |
| 研究领域[WOS] | Chemistry |
| 关键词[WOS] | NUCLEAR-MAGNETIC-RESONANCE ; 7-HELICAL TRANSMEMBRANE PROTEIN ; COLI DIACYLGLYCEROL KINASE ; CHANNEL-FORMING DOMAIN ; ANGLE-SPINNING NMR ; CHEMICAL-SHIFT ; LIPID-BILAYERS ; BIOLOGICAL-MEMBRANES ; ESCHERICHIA-COLI ; INFLUENZA-A |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000340443100003 |
| 公开日期 | 2015-07-14 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/1335]  |
| 专题 | 武汉物理与数学研究所_磁共振基础研究部 |
| 作者单位 | Chinese Acad Sci, Wuhan Inst Phys & Math, Wuhan Ctr Magnet Resonance, Key Lab Magnet Resonance Biol Syst,State Key Lab, Wuhan 430071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Zhengfeng,Chen, Yanke,Tang, Xinqi,et al. Solid-State NMR Shows That Dynamically Different Domains of Membrane Proteins Have Different Hydration Dependence[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2014,118(32):9553-9564. |
| APA | Zhang, Zhengfeng,Chen, Yanke,Tang, Xinqi,Li, Jianping,Wang, Liying,&Yang, Jun.(2014).Solid-State NMR Shows That Dynamically Different Domains of Membrane Proteins Have Different Hydration Dependence.JOURNAL OF PHYSICAL CHEMISTRY B,118(32),9553-9564. |
| MLA | Zhang, Zhengfeng,et al."Solid-State NMR Shows That Dynamically Different Domains of Membrane Proteins Have Different Hydration Dependence".JOURNAL OF PHYSICAL CHEMISTRY B 118.32(2014):9553-9564. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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