Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.
Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.
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DOI：
10.1021/acs.chemrev.2c00600
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发表时间：
2023-03-22
期刊：
影响因子：
62.1
通讯作者：
Barran, Perdita
中科院分区：
文献类型：
--
作者：
Christofi, Emilia;Barran, Perdita
在过去的二十年里，用离子迁移质谱仪(IM-MS)技术对大分子生物分子的研究为结构生物学领域提供了实质性的见解。应用于给定目标分析物的IM-MS工作流程提供质量、电荷和构象，并且所有这三个都可用于识别结构信息。虽然质量和电荷在质谱学中是确定的，但由于离子迁移率的增加，使得同分异构体和同压异构体离子的分离和构象的直接确定成为可能，这为结构生物学带来了巨大的好处。在这篇综述中，我们将重点放在蛋白质及其络合物的分析上，我们从样品的制备、离子的产生以及它们在不同迁移率和质谱仪中的分离来概述IM-MS实验的典型特征。我们描述了从蛋白质构象的角度对离子迁移率数据的解释，以及如何使用计算工具将数据与来自其他来源的数据进行比较。结合最近的例子，详细说明了通过与气体或表面或光子光活化的碰撞将迁移率分析耦合到活化的好处。最后，我们专注于IM-MS实验在应用于构象动态和本质无序蛋白质的研究中所提供的见解。
The investigation of macromolecular biomolecules with ion mobility mass spectrometry (IM-MS) techniques has provided substantial insights into the field of structural biology over the past two decades. An IM-MS workflow applied to a given target analyte provides mass, charge, and conformation, and all three of these can be used to discern structural information. While mass and charge are determined in mass spectrometry (MS), it is the addition of ion mobility that enables the separation of isomeric and isobaric ions and the direct elucidation of conformation, which has reaped huge benefits for structural biology. In this review, where we focus on the analysis of proteins and their complexes, we outline the typical features of an IM-MS experiment from the preparation of samples, the creation of ions, and their separation in different mobility and mass spectrometers. We describe the interpretation of ion mobility data in terms of protein conformation and how the data can be compared with data from other sources with the use of computational tools. The benefit of coupling mobility analysis to activation via collisions with gas or surfaces or photons photoactivation is detailed with reference to recent examples. And finally, we focus on insights afforded by IM-MS experiments when applied to the study of conformationally dynamic and intrinsically disordered proteins.
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影响因子：
16.6
作者：
Allison TM;Reading E;Liko I;Baldwin AJ;Laganowsky A;Robinson CV
通讯作者：
Robinson CV
影响因子：
7.4
作者：
Baird, Matthew A.;Anderson, Gordon A.;Shvartsburg, Alexandre A.
通讯作者：
Shvartsburg, Alexandre A.
改善了基于Q-TOF仪器的实用电子碎片，改善了蛋白质和PTM表征。
DOI：
10.1021/jasms.0c00482
发表时间：
2021-08-04
影响因子：
3.2
作者：
Beckman JS;Voinov VG;Hare M;Sturgeon D;Vasil'ev Y;Oppenheimer D;Shaw JB;Wu S;Glaskin R;Klein C;Schwarzer C;Stafford G
通讯作者：
Stafford G
影响因子：
4.2
作者：
Allen, Samuel J.;Giles, Kevin;Bush, Matthew F.
通讯作者：
Bush, Matthew F.
影响因子：
2
作者：
Barnett, DA;Ding, LY;Guevremont, R
通讯作者：
Guevremont, R