A Flexible, Modular Platform for Multidimensional Ion Mobility of Native-like Ions.
A Flexible, Modular Platform for Multidimensional Ion Mobility of Native-like Ions.
复制标题
用于类原生离子多维离子淌度的灵活模块化平台。
DOI：
10.1021/jasms.3c00112
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发表时间：
2023
影响因子：
3.2
通讯作者：
Bush,MatthewF
中科院分区：
文献类型：
--
作者：
Eaton,RachelM;Zercher,BenjaminP;Wageman,AnneClaire;Bush,MatthewF
天然离子迁移率（IM）质谱（MS）用于探测生物分子复合物的大小、形状和组装。IM-IM-MS可以通过分离结构亚群进行进一步分析来增加结构研究中可用的信息量。此前，IM-IM-MS已经使用结构无损离子操作（SLIM）架构来探测气相蛋白质离子的结构稳定性。本文以SLIM器件为基础，构建了一种具有多种工作模式的多维IM仪器。在这种新设计中，模块化装置用于执行所有离子操作，包括初始积累、注入、分离、选择和捕获。使用一维IM，确定了一组原生离子的碰撞截面（Ω）值。这些Ω值与以前使用限制射频漂移电池测量的值相差3%以内。串联IM实验在包含紧凑和部分展开结构的泛素离子样品上进行，证明该平台可以分离结构的亚群。最后，使用该平台演示了其他分析模式，包括复用IM和逆IM。该平台能够在不同的IM分析模式之间快速切换，使其成为研究蛋白质结构和动力学的高度灵活的工具。
Native ion mobility (IM) mass spectrometry (MS) is used to probe the size, shape, and assembly of biomolecular complexes. IM-IM-MS can increase the amount of information available in structural studies by isolating subpopulations of structures for further analysis. Previously, IM-IM-MS has been implemented using the Structures for Lossless Ion Manipulations (SLIM) architecture to probe the structural stability of gas-phase protein ions. Here, a new multidimensional IM instrument constructed from SLIM devices is characterized using multiple operational modes. In this new design, modular devices are used to perform all ion manipulations, including initial accumulation, injection, separation, selection, and trapping. Using single-dimension IM, collision cross section (Ω) values are determined for a set of native-like ions. These Ω values are within 3% of those reported previously based on measurements using RF-confining drift cells. Tandem IM experiments are performed on a sample of ubiquitin ions that contains both compact and partially unfolded structures, demonstrating that this platform can isolate subpopulations of structures. Finally, additional modes of analysis, including multiplexed IM and inverse IM, are demonstrated using this platform. The ability of this platform to quickly switch between different modes of IM analysis makes it a highly flexible tool for studying protein structures and dynamics.