High-resolution mass spectrometry of small molecules bound to membrane proteins

被引：0
|
作者：
Gault J. [1 ]
Donlan J.A.C. [1 ]
Liko I. [1 ]
Hopper J.T.S. [1 ]
Gupta K. [1 ]
Housden N.G. [2 ]
Struwe W.B. [1 ]
Marty M.T. [1 ]
Mize T. [1 ]
Bechara C. [1 ,5 ]
Zhu Y. [3 ]
Wu B. [3 ]
Kleanthous C. [2 ]
Belov M. [4 ]
Damoc E. [4 ]
Makarov A. [4 ]
Robinson C.V. [1 ]
机构：
[1] Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford
[2] Department of Biochemistry, University of Oxford, Oxford
[3] CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Pudong
[4] Thermo Fisher Scientific, Bremen
[5] UMR 5235 CNRS, Université de Montpellier, Montpellier
来源：
Nature Methods | 2016年 / 13卷 / 4期
基金：
英国惠康基金; 英国生物技术与生命科学研究理事会; 英国医学研究理事会;
关键词：
D O I：
10.1038/nmeth.3771
中图分类号：
学科分类号：
摘要：
Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry-based method for analyzing intact membrane protein-ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length. © 2016 Nature America, Inc. All rights reserved.
引用
收藏
页码：333 / 336
页数：3
相关论文
共 50 条
12345