Interrogating Membrane Protein Structure and Lipid Interactions by Native Mass Spectrometry.

Interrogating Membrane Protein Structure and Lipid Interactions by Native Mass Spectrometry.
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通过天然质谱分析膜蛋白结构和脂质相互作用。

DOI:
10.1007/978-1-0716-0724-4_11
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发表时间:
2020
期刊:
Methods in molecular biology (Clifton, N.J.)
影响因子:
--
通讯作者:
Hammerschmid D
Hammerschmid D
中科院分区:
--
文献类型:
--
作者:
Hammerschmid D

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本机质谱和本机离子迁移率质谱是结构生物学中现已建立的技术,最近的工作开发了这些方法,用于研究在脂质双层和洗涤剂环境中重建的整合膜蛋白。在这里,我们展示了如何原生质谱可以用来询问完整的膜蛋白,提供见解的构象,寡聚化,亚基组成/化学计量,以及与洗涤剂/脂质/药物的相互作用。此外,我们讨论了样品的要求和实验的考虑,独特的整体膜蛋白质本机质谱研究。
Native mass spectrometry and native ion mobility mass spectrometry are now established techniques in structural biology, with recent work developing these methods for the study of integral membrane proteins reconstituted in both lipid bilayer and detergent environments. Here we show how native mass spectrometry can be used to interrogate integral membrane proteins, providing insights into conformation, oligomerization, subunit composition/stoichiometry, and interactions with detergents/lipids/drugs. Furthermore, we discuss the sample requirements and experimental considerations unique to integral membrane protein native mass spectrometry research.
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