An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins.

An Adaptable Phospholipid Membrane Mimetic System for Solution NMR Studies of Membrane Proteins.
复制标题

DOI:
10.1021/jacs.7b06730
复制
发表时间:
2017-10-25
影响因子:
15
通讯作者:
Nietlispach D
Nietlispach D
中科院分区:
化学1区
文献类型:
--
作者:
Chien CH;Helfinger LR;Bostock MJ;Solt A;Tan YL;Nietlispach D

文献摘要

参考文献

被引文献

相似文献

基于saposin-A(SapA)支架蛋白,我们证明了适合的大小适应性磷脂膜模拟系统的溶液NMR研究膜蛋白(MP)在接近天然条件下。Salipro纳米颗粒尺寸可以通过调节鞘脂激活蛋白与脂质的化学计量在宽的pH范围内调节,使得能够在Salipro纳米颗粒中维持足够高量的磷脂以模拟真实的膜环境,同时控制总体尺寸以使得能够对一系列MP进行溶液NMR。三个代表性的MP,包括一个G-蛋白偶联受体,成功地纳入SapA-二肉豆蔻酰磷脂酰胆碱纳米颗粒,并通过溶液NMR光谱研究。
Based on the saposin-A (SapA) scaffold protein, we demonstrate the suitability of a size-adaptable phospholipid membrane-mimetic system for solution NMR studies of membrane proteins (MPs) under close-to-native conditions. The Salipro nanoparticle size can be tuned over a wide pH range by adjusting the saposin-to-lipid stoichiometry, enabling maintenance of sufficiently high amounts of phospholipid in the Salipro nanoparticle to mimic a realistic membrane environment while controlling the overall size to enable solution NMR for a range of MPs. Three representative MPs, including one G-protein-coupled receptor, were successfully incorporated into SapA-dimyristoylphosphatidylcholine nanoparticles and studied by solution NMR spectroscopy.
DOI: 10.1038/nsmb.1807
发表时间: 2010-06
影响因子: 16.8
作者:
通讯作者: --
DOI: 10.1007/s10858-014-9883-6
发表时间: 2015-04
影响因子: 2.7
作者:
Hagn, Franz;Wagner, Gerhard
通讯作者: Wagner, Gerhard
DOI: 10.1002/pro.5560070420
发表时间: 1998-04-01
期刊: PROTEIN SCIENCE
影响因子: 8
作者:
Wallin, E;von Heijne, G
通讯作者: von Heijne, G
DOI: 10.1016/j.str.2013.01.005
发表时间: 2013-03-05
期刊: STRUCTURE
影响因子: 5.7
作者:
Etzkorn, Manuel;Raschle, Thomas;Wagner, Gerhard
通讯作者: Wagner, Gerhard
DOI: 10.1038/nmeth.3801
发表时间: 2016-04
期刊: Nature methods
影响因子: 48
作者:
Frauenfeld J;Löving R;Armache JP;Sonnen AF;Guettou F;Moberg P;Zhu L;Jegerschöld C;Flayhan A;Briggs JA;Garoff H;Löw C;Cheng Y;Nordlund P
通讯作者: Nordlund P