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Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein–Protein Interactions─A Method for All Seasons
Chemical Reviews ( IF 51.4 ) Pub Date : 2021-11-19 , DOI: 10.1021/acs.chemrev.1c00786
Lolita Piersimoni 1, 2 , Panagiotis L Kastritis 3, 4, 5 , Christian Arlt 1, 2 , Andrea Sinz 1, 2
Affiliation  

Mass spectrometry (MS) has become one of the key technologies of structural biology. In this review, the contributions of chemical cross-linking combined with mass spectrometry (XL-MS) for studying three-dimensional structures of proteins and for investigating protein–protein interactions are outlined. We summarize the most important cross-linking reagents, software tools, and XL-MS workflows and highlight prominent examples for characterizing proteins, their assemblies, and interaction networks in vitro and in vivo. Computational modeling plays a crucial role in deriving 3D-structural information from XL-MS data. Integrating XL-MS with other techniques of structural biology, such as cryo-electron microscopy, has been successful in addressing biological questions that to date could not be answered. XL-MS is therefore expected to play an increasingly important role in structural biology in the future.

中文翻译:

用于研究蛋白质构象和蛋白质-蛋白质相互作用的交联质谱——一种四季皆宜的方法

质谱(MS)已成为结构生物学的关键技术之一。在这篇综述中,概述了化学交联结合质谱 (XL-MS) 在研究蛋白质的三维结构和研究蛋白质-蛋白质相互作用方面的贡献。我们总结了最重要的交联试剂、软件工具和 XL-MS 工作流程,并重点介绍了表征蛋白质、它们的组装和体外体内相互作用网络的突出示例. 计算建模在从 XL-MS 数据中获取 3D 结构信息方面起着至关重要的作用。将 XL-MS 与其他结构生物学技术(如低温电子显微镜)相结合,已成功解决了迄今为止无法回答的生物学问题。因此,XL-MS 有望在未来在结构生物学中发挥越来越重要的作用。
更新日期:2021-11-19
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