Bayer Peter, Matena Anja, Beuck Christine
Structural and Medicinal Biochemistry, University of Duisburg-Essen, Universitätsstr. 1-5, 45141 Essen, Germany.
Beilstein J Org Chem. 2020 Oct 9;16:2505-2522. doi: 10.3762/bjoc.16.203. eCollection 2020.
As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small binding pockets in proteins to recognizing patches on protein surfaces, mostly via supramolecular chemistry, with the goal to modulate protein-protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor.
作为少数能够提供原子分辨率的分析方法之一,核磁共振光谱法是研究蛋白质与其相互作用伙伴(包括生物分子和合成配体)之间相互作用的宝贵工具。近年来,化学领域的研究重点不断扩展,从靶向蛋白质中的小结合口袋转向识别蛋白质表面的区域,主要通过超分子化学来实现,目的是调节蛋白质-蛋白质相互作用。在此,我们介绍已应用于表征这些分子相互作用的核磁共振方法,并讨论这一研究工作所面临的挑战。