串联陷阱离子淌度谱/质谱联用（TIMS/MS）：一种用于研究异质样品的很有前途的分析方法。
Tandem-trapped ion mobility spectrometry/mass spectrometry (TIMS/MS): a promising analytical method for investigating heterogenous samples.
机构信息
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306-4390, USA.
Bruker Daltonics Inc., Billerica, MA 01821, USA.
出版信息
Analyst. 2022 May 30;147(11):2317-2337. doi: 10.1039/d2an00335j.
Abstract
Ion mobility spectrometry/mass spectrometry (IMS/MS) is widely used to study various levels of protein structure. Here, we review the current state of affairs in -trapped ion mobility spectrometry/mass spectrometry (TIMS/MS). Two different TIMS/MS instruments are discussed in detail: the first TIMS/MS instrument, constructed from coaxially aligning two TIMS devices; and an orthogonal TIMS/MS configuration that comprises an ion trap for irradiation of ions with UV photons. We discuss the various workflows the two TIMS/MS setups offer and how these can be used to study primary, tertiary, and quaternary structures of protein systems. We also discuss, from a more fundamental perspective, the processes that lead to denaturation of protein systems in TIMS/MS and how to soften the measurement so that biologically meaningful structures can be characterised with TIMS/MS. We emphasize the concepts underlying TIMS/MS to underscore the opportunities tandem-ion mobility spectrometry methods offer for investigating heterogeneous samples.
摘要
离子淌度谱/质谱联用（IMS/MS）广泛用于研究各种水平的蛋白质结构。在这里，我们回顾了 - 内离子淌度谱/质谱联用（TIMS/MS）的现状。详细讨论了两种不同的 TIMS/MS 仪器：第一个 TIMS/MS 仪器由同轴对准的两个 TIMS 装置构成；以及一种正交 TIMS/MS 配置，包括一个离子阱，用于用紫外光子辐照离子。我们讨论了这两种 TIMS/MS 装置提供的各种工作流程，以及如何利用这些流程研究蛋白质系统的一级、三级和四级结构。我们还从更基础的角度讨论了导致蛋白质系统在 TIMS/MS 中变性的过程，以及如何软化测量，以便使用 TIMS/MS 来表征具有生物学意义的结构。我们强调了 TIMS/MS 的基本概念，以强调串联离子淌度谱方法在研究异质样品方面提供的机会。
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