Protein-protein interactions involving intrinsically disordered proteins (IDPs) usually display dynamic and multivalent features. Recent experimental data revealed myriad functional roles of the dynamic multivalent interaction (DMI) of IDPs. However, characterization of DMI remains a challenge due to its complex and promiscuous nature. Recent studies start showing that understanding the mechanistic role of DMI relies on combined use of various techniques and construction of microscopic models in elucidating the binding thermodynamics and kinetics.

中文翻译：

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内在无序的蛋白质的动态多价相互作用。

涉及内在无序蛋白（IDP）的蛋白-蛋白相互作用通常表现出动态和多价特征。最近的实验数据揭示了IDP的动态多价相互作用（DMI）的多种功能作用。然而，由于DMI的复杂性和混杂性，其表征仍然是一个挑战。最近的研究开始表明，了解DMI的机械作用取决于阐明结合热力学和动力学的各种技术的结合使用和微观模型的构建。