Theory Department, National Institute of Chemistry, 1000 Ljubljana, Slovenia.
Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, 1000 Ljubljana, Slovenia.
Front Biosci (Landmark Ed). 2023 Aug 28;28(8):183. doi: 10.31083/j.fbl2808183.
Similar to other polypeptides and electrolytes, proteins undergo phase transitions, obeying physicochemical laws. They can undergo liquid-to-gel and liquid-to-liquid phase transitions. Intrinsically disordered proteins are particularly susceptible to phase separation. After a general introduction, the principles of studies of protein folding, aggregation, and condensation are described. Numerous recent and older studies have confirmed that the process of liquid-liquid phase separation (LLPS) leads to various condensed bodies in cells, which is one way cells manage stress. We review what is known about protein aggregation and condensation in the cell, notwithstanding the protective and pathological roles of protein aggregates. This includes membrane-less organelles and cytotoxicity of the prefibrillar oligomers of amyloid-forming proteins. We then describe and evaluate bioinformatic () methods for predicting protein aggregation-prone regions of proteins that form amyloids, prions, and condensates.
类似于其他多肽和电解质，蛋白质也会发生相变，遵循物理化学规律。它们可以经历液相到凝胶相和液相到液相的转变。无规卷曲的蛋白质特别容易发生相分离。在一般性介绍之后，描述了研究蛋白质折叠、聚集和凝聚的原理。许多最近和较早的研究证实，液-液相分离（LLPS）过程导致细胞中出现各种凝聚体，这是细胞应对压力的一种方式。我们回顾了关于细胞中蛋白质聚集和凝聚的已知知识，尽管蛋白质聚集体具有保护和病理作用。这包括无膜细胞器和淀粉样蛋白形成蛋白的前纤维寡聚物的细胞毒性。然后，我们描述和评估了用于预测形成淀粉样蛋白、朊病毒和凝聚物的蛋白质的易于聚集的区域的生物信息学方法。
