Department of Chemistry, University of Massachusetts, Amherst, MA 01003, U.S.A.
Biochem Soc Trans. 2024 Feb 28;52(1):319-329. doi: 10.1042/BST20230618.
Intrinsically disordered proteins (IDPs) are one of the major drivers behind the formation and characteristics of biomolecular condensates. Due to their inherent flexibility, the backbones of IDPs are significantly exposed, rendering them highly influential and susceptible to biomolecular phase separation. In densely packed condensates, exposed backbones have a heightened capacity to interact with neighboring protein chains, which might lead to strong coupling between the secondary structures and phase separation and further modulate the subsequent transitions of the condensates, such as aging and fibrillization. In this mini-review, we provide an overview of backbone-mediated interactions and secondary structures within biomolecular condensates to underscore the importance of protein backbones in phase separation. We further focus on recent advances in experimental techniques and molecular dynamics simulation methods for probing and exploring the roles of backbone interactions and secondary structures in biomolecular phase separation involving IDPs.
无规卷曲蛋白质（IDPs）是生物分子凝聚物形成和特征的主要驱动因素之一。由于其固有灵活性，IDP 的骨架明显暴露，使其具有高度影响力并易受生物分子相分离的影响。在密集的凝聚物中，暴露的骨架具有与相邻蛋白质链相互作用的更高能力，这可能导致二级结构和相分离之间的强耦合，并进一步调节凝聚物的后续转变，例如老化和纤维化。在这篇迷你综述中，我们概述了生物分子凝聚物中骨架介导的相互作用和二级结构，以强调蛋白质骨架在相分离中的重要性。我们进一步关注用于探测和探索涉及 IDP 的生物分子相分离中骨架相互作用和二级结构作用的最新实验技术和分子动力学模拟方法的进展。
