Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120, Halle (Saale), Germany.
Angew Chem Int Ed Engl. 2018 May 28;57(22):6390-6396. doi: 10.1002/anie.201709559. Epub 2018 Apr 19.
Structural mass spectrometry (MS) is gaining increasing importance for deriving valuable three-dimensional structural information on proteins and protein complexes, and it complements existing techniques, such as NMR spectroscopy and X-ray crystallography. Structural MS unites different MS-based techniques, such as hydrogen/deuterium exchange, native MS, ion-mobility MS, protein footprinting, and chemical cross-linking/MS, and it allows fundamental questions in structural biology to be addressed. In this Minireview, I will focus on the cross-linking/MS strategy. This method not only delivers tertiary structural information on proteins, but is also increasingly being used to decipher protein interaction networks, both in vitro and in vivo. Cross-linking/MS is currently one of the most promising MS-based approaches to derive structural information on very large and transient protein assemblies and intrinsically disordered proteins.
结构质谱（MS）在获取有关蛋白质和蛋白质复合物有价值的三维结构信息方面变得越来越重要，它补充了现有的技术，如 NMR 光谱学和 X 射线晶体学。结构 MS 结合了不同的基于 MS 的技术，如氢/氘交换、天然 MS、离子迁移率 MS、蛋白质足迹和化学交联/ MS，它允许解决结构生物学中的基本问题。在这篇综述中，我将重点介绍交联/ MS 策略。该方法不仅提供蛋白质的三级结构信息，而且越来越多地用于解析体外和体内的蛋白质相互作用网络。交联/ MS 目前是基于 MS 的最有前途的方法之一，可用于推导非常大的和瞬态蛋白质组装体以及固有无序蛋白质的结构信息。
