Sinz Andrea, Arlt Christian, Chorev Dror, Sharon Michal
Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, D-06120, Halle, Germany.
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, 76100, Israel.
Protein Sci. 2015 Aug;24(8):1193-209. doi: 10.1002/pro.2696. Epub 2015 May 27.
Mass spectrometry (MS) is becoming increasingly popular in the field of structural biology for analyzing protein three-dimensional-structures and for mapping protein-protein interactions. In this review, the specific contributions of chemical crosslinking and native MS are outlined to reveal the structural features of proteins and protein assemblies. Both strategies are illustrated based on the examples of the tetrameric tumor suppressor protein p53 and multisubunit vinculin-Arp2/3 hybrid complexes. We describe the distinct advantages and limitations of each technique and highlight synergistic effects when both techniques are combined. Integrating both methods is especially useful for characterizing large protein assemblies and for capturing transient interactions. We also point out the future directions we foresee for a combination of in vivo crosslinking and native MS for structural investigation of intact protein assemblies.
质谱（MS）在结构生物学领域正变得越来越流行，用于分析蛋白质三维结构和绘制蛋白质-蛋白质相互作用图谱。在本综述中，概述了化学交联和天然质谱的具体贡献，以揭示蛋白质和蛋白质组装体的结构特征。基于四聚体肿瘤抑制蛋白p53和多亚基纽蛋白-Arp2/3杂合复合物的例子说明了这两种策略。我们描述了每种技术的独特优点和局限性，并强调了两种技术结合时的协同效应。整合这两种方法对于表征大型蛋白质组装体和捕捉瞬时相互作用特别有用。我们还指出了我们预见到的体内交联和天然质谱相结合用于完整蛋白质组装体结构研究的未来方向。
