Intrinsically disordered proteins (IDPs) exploit their plasticity to deploy a rich panoply of soft interactions and binding phenomena. Advances in tailoring molecular simulations for IDPs combined with experimental cross-validation offer an atomistic view of the mechanisms that control IDP binding, function, and dysfunction. The emerging theme is that unbound IDPs autonomously form transient local structures and self-interactions that determine their binding behavior. Recent results have shed light on whether and how IDPs fold, stay disordered or drive condensation upon binding; how they achieve binding specificity and select among competing partners. The disorder-binding paradigm is now being proactively used by researchers to target IDPs for rational drug design and engineer molecular responsive elements for biosensing applications.

本质无序蛋白 (IDP) 利用其可塑性来部署丰富的软相互作用和结合现象。 IDP 分子模拟与实验交叉验证相结合的进展为控制 IDP 结合、功能和功能障碍的机制提供了原子论观点。新出现的主题是，不受束缚的国内流离失所者自主地形成决定其束缚行为的短暂局部结构和自我相互作用。最近的结果揭示了 IDP 是否以及如何折叠、保持无序或在结合时驱动凝结；他们如何实现结合特异性并在竞争伙伴中进行选择。研究人员现在正在积极使用障碍结合范式来针对 IDP 进行合理的药物设计，并为生物传感应用设计分子响应元件。