Public Higher Medical Professional School in Opole, Katowicka 68, 45060 Opole, Poland.
Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50383 Wroclaw, Poland.
J Inorg Biochem. 2019 Oct;199:110783. doi: 10.1016/j.jinorgbio.2019.110783. Epub 2019 Jul 16.
Protein-protein interactions play important roles for a variety of cell functions, often involving metal ions; in fact, metal-ion binding mediates and regulates the activity of a wide range of biomolecules. Enlightening all of the specific features of metal-protein and metal-mediated protein-protein interactions can be a very challenging task; a detailed knowledge of the thermodynamic and spectroscopic parameters and the structural changes of the protein is normally required. For this purpose, many experimental techniques are employed, embracing all fields of Analytical and Bioinorganic Chemistry. In addition, the use of peptide models, reproducing the primary sequence of the metal-binding sites, is also proved to be useful. In this paper, a review of the most useful techniques for studying ligand-protein interactions with a special emphasis on metal-protein interactions is provided, with a critical summary of their strengths and limitations.
蛋白质-蛋白质相互作用在各种细胞功能中起着重要作用,通常涉及金属离子;事实上,金属离子结合介导和调节广泛的生物分子的活性。阐明金属-蛋白质和金属介导的蛋白质-蛋白质相互作用的所有特定特征可能是一项非常具有挑战性的任务;通常需要详细了解蛋白质的热力学和光谱参数以及结构变化。为此,采用了许多实验技术,涵盖了分析和生物无机化学的所有领域。此外,使用肽模型来复制金属结合位点的一级序列也被证明是有用的。在本文中,提供了一种用于研究配体-蛋白质相互作用的最有用技术的综述,特别强调了金属-蛋白质相互作用,并对其优缺点进行了批判性总结。