Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin
文献类型：期刊论文
| 作者 | Iuga, Dinu1; Ding, Xiaoyan2; Wang, Honglei4; Peng, Bo2; Cui, Haolin2; Gao, Yujiao2; Judge, Peter J.3; Li, Guohui4; Watts, Anthony3; Zhao, Xin2 |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
 |
| 出版日期 | 2016-11-01 |
| 卷号 | 1857期号:11页码:1786-1795 |
| 关键词 | Electrostatic Coupling Functional Conformational Change Aromatic Residue Mutational Analysis And Functional Assays Solid-state Nmr |
| ISSN号 | 0005-2728 |
| DOI | 10.1016/j.bbabio.2016.08.002 |
| 文献子类 | Article |
| 英文摘要 | Electrostatic coupling leading to conformational changes in proteins is challenging to demonstrate directly, it requires that both the local, discrete electronic details and dynamic information relevant to the functional descriptions are probed. Here, as a novel study to address this challenge, the roles of an aromatic residue in influencing the functional conformational changes of a membrane receptor in its natural membrane environment are reported. Previously intractable discrete electronic details have been obtained using 2D solid-state NMR of specifically labelled receptor, reinforced with molecular dynamic simulations, mutational analysis and functional assays, supported by and compared with rigid-atom crystal structural models. Hydrogen bonding and hydrophobic interactions are identified as the mechanistic origin for direct electromechanical coupling to the dynamics of conformational changes within the receptor. (C) 2016 Elsevier B.V. All rights reserved. |
| WOS关键词 | SOLID-STATE NMR ; DARK-ADAPTED BACTERIORHODOPSIN ; MOLECULAR-DYNAMICS ; PURPLE MEMBRANE ; C-13 NMR ; ANGSTROM RESOLUTION ; CROSS-POLARIZATION ; HALOBACTERIUM-HALOBIUM ; CRYSTAL-STRUCTURE ; LOW-TEMPERATURE |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000384867400008 |
| 出版者 | ELSEVIER SCIENCE BV |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/169870]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 通讯作者 | Li, Guohui; Watts, Anthony; Zhao, Xin |
| 作者单位 | 1.Univ Warwick, Dept Phys, UK MHz Solid State NMR Facil 850, Coventry CV4 7AL, W Midlands, England 2.East China Normal Univ, Shanghai Key Lab Magnet Resonance, Dept Phys, Shanghai 200062, Peoples R China 3.Univ Oxford, Dept Biochem, Biomembrane Struct Unit, South Parks Rd, Oxford OX1 3QU, England 4.Chinese Acad Sci, State Key Lab Mol React Dynam, Inst Chem Phys, Dalian 116023, Liaoning, Peoples R China |
| 推荐引用方式 GB/T 7714 | Iuga, Dinu,Ding, Xiaoyan,Wang, Honglei,et al. Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2016,1857(11):1786-1795. |
| APA | Iuga, Dinu.,Ding, Xiaoyan.,Wang, Honglei.,Peng, Bo.,Cui, Haolin.,...&Zhao, Xin.(2016).Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin.BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,1857(11),1786-1795. |
| MLA | Iuga, Dinu,et al."Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1857.11(2016):1786-1795. |
入库方式： OAI收割
来源：大连化学物理研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。