傅里叶变换离子回旋共振
化学
质谱法
蛋白质组学
自上而下的蛋白质组学
高分子
红外多光子离解
电子俘获离解
蛋白质亚单位
结构生物学
离子回旋共振
序列(生物学)
计算生物学
串联质谱法
分析化学(期刊)
蛋白质质谱法
色谱法
生物化学
离子
回旋加速器
生物
基因
有机化学
作者
Huilin Li,Hong Hanh Nguyen,Rachel R. Ogorzalek Loo,Iain D. G. Campuzano,Joseph A. Loo
出处
期刊:Nature Chemistry
[Springer Nature]
日期:2018-01-01
卷期号:10 (2): 139-148
被引量:213
摘要
Mass spectrometry (MS) has become a crucial technique for the analysis of protein complexes. Native MS has traditionally examined protein subunit arrangements, while proteomics MS has focused on sequence identification. These two techniques are usually performed separately without taking advantage of the synergies between them. Here we describe the development of an integrated native MS and top-down proteomics method using Fourier-transform ion cyclotron resonance (FTICR) to analyse macromolecular protein complexes in a single experiment. We address previous concerns of employing FTICR MS to measure large macromolecular complexes by demonstrating the detection of complexes up to 1.8 MDa, and we demonstrate the efficacy of this technique for direct acquirement of sequence to higher-order structural information with several large complexes. We then summarize the unique functionalities of different activation/dissociation techniques. The platform expands the ability of MS to integrate proteomics and structural biology to provide insights into protein structure, function and regulation.
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