基于离子迁移谱-质谱(IMS-MS)技术的高阶蛋白质结构研究进展

IF 0.4 Q4 SPECTROSCOPY
Jongcheol Seo
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引用次数: 0

摘要

尽管质谱法在蛋白质组学领域取得了巨大的成功,但它在确定肽、蛋白质及其组装的结构细节方面的应用有限。新兴的离子迁移谱-质谱使我们能够探索蛋白质离子在气相中的构象空间,并且进一步结合气相离子光谱和碰撞诱导展开扩展了其阐明二级结构和构象转变的局部细节的能力。本文将简要介绍IMS-MS与气相离子红外光谱或碰撞诱导展开相结合的方法,以及它们最近成功揭示高阶结构细节的结果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Advances in Ion Mobility Spectrometry-Mass Spectrometry (IMS-MS)-Based Techniques for Elucidating Higher-Order Protein Structures
Despite its great success in the field of proteomics, mass spectrometry has limited use for determining structural details of peptides, proteins, and their assemblies. Emerging ion mobility spectrometry-mass spectrometry has enabled us to explore the conformational space of protein ions in the gas phase, and further combinations with the gas-phase ion spectroscopy and the collision-induced unfolding have extended its abilities to elucidating the secondary structure and local details of conformational transitions. This review will provide a brief introduction to the combined approaches of IMS-MS with gas-phase ion infrared spectroscopy or collision-induced unfolding and their most recent results that successfully revealed higher-order structural details.
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来源期刊
CiteScore
0.90
自引率
20.00%
发文量
0
审稿时长
6 weeks
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