Ion mobility-mass spectrometry as a tool to investigate protein-ligand interactions

被引：31
作者：
Goeth, Melanie [1 ,2 ]
Pagel, Kevin [1 ,2 ]
机构：
[1] Free Univ Berlin, Inst Chem & Biochem, Takustr 3, D-14195 Berlin, Germany
[2] Max Planck Gesell, Fritz Haber Inst, Dept Mol Phys, Faradayweg 4-6, D-14195 Berlin, Germany
来源：
ANALYTICAL AND BIOANALYTICAL CHEMISTRY | 2017年 / 409卷 / 18期
关键词：
Ion mobility-mass spectrometry; Protein-ligand complexes; Native mass spectrometry; Noncovalent complexes; Catch and release; Collision-induced unfolding; PHASE STRUCTURAL BIOLOGY; COLLISION CROSS-SECTIONS; GAS-PHASE; ELECTROSPRAY-IONIZATION; CARBONIC-ANHYDRASE; MEMBRANE-PROTEINS; DRUG DISCOVERY; BINDING; COMPLEXES; ASSAY;
D O I：
10.1007/s00216-017-0384-9
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Ion mobility-mass spectrometry (IM-MS) is a powerful tool for the simultaneous analysis of mass, charge, size, and shape of ionic species. It allows the characterization of even low-abundant species in complex samples and is therefore particularly suitable for the analysis of proteins and their assemblies. In the last few years even complex and intractable species have been investigated successfully with IM-MS and the number of publications in this field is steadily growing. This trend article highlights recent advances in which IM-MS was used to study protein-ligand complexes and in particular focuses on the catch and release (CaR) strategy and collision-induced unfolding (CIU).
引用
收藏
页码：4305 / 4310
页数：6
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