National Key Laboratory of Agricultural Microbiology, Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Rev Recent Clin Trials. 2024;19(3):176-188. doi: 10.2174/0115748871271420240213064251.
Intrinsically Disordered Proteins (IDPs) are active in different cellular procedures like ordered assembly of chromatin and ribosomes, interaction with membrane, protein, and ligand binding, molecular recognition, binding, and transportation nuclear pores, microfilaments and microtubules process and disassembly, protein functions, RNA chaperone, and nucleic acid binding, modulation of the central dogma, cell cycle, and other cellular activities, post-translational qualification and substitute splicing, and flexible entropic linker and management of signaling pathways.
The intrinsic disorder is a precise structural characteristic that permits IDPs/IDPRs to be involved in both one-to-many and many-to-one signaling. IDPs/IDPRs also exert some dynamical and structural ordering, being much less constrained in their activities than folded proteins. Nuclear magnetic resonance (NMR) spectroscopy is a major technique for the characterization of IDPs, and it can be used for dynamic and structural studies of IDPs.
This review was carried out to discuss intrinsically disordered proteins and their different goals, as well as the importance and effectiveness of NMR in characterizing intrinsically disordered proteins in healthy and diseased states.
无序蛋白质（IDPs）在不同的细胞过程中发挥作用，如染色质和核糖体的有序组装、与膜、蛋白质和配体的相互作用、分子识别、结合和运输核孔、微丝和微管的过程和拆卸、蛋白质功能、RNA 伴侣和核酸结合、中心法则的调节、细胞周期和其他细胞活动、翻译后修饰和替代剪接，以及灵活的熵链接和信号通路的管理。
无序是一种精确的结构特征，允许 IDPs/IDPRs 参与一对一和一对多的信号传递。IDPs/IDPRs 也表现出一些动力学和结构有序性，其活性比折叠蛋白质受限制小得多。核磁共振（NMR）光谱是鉴定 IDPs 的主要技术，可用于 IDPs 的动力学和结构研究。
本综述旨在讨论无序蛋白质及其不同的目标，以及 NMR 在鉴定健康和患病状态下无序蛋白质的重要性和有效性。
