School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.
Bioinformatics Institute, Agency for Science, Technology, and Research (A*STAR), Singapore, 138671, Singapore.
Sci Rep. 2021 May 11;11(1):9930. doi: 10.1038/s41598-021-88992-0.
Charge is a key determinant of intrinsically disordered protein (IDP) and intrinsically disordered region (IDR) properties. IDPs and IDRs are enriched in sites of phosphorylation, which alters charge. Visualizing the degree to which phosphorylation modulates the charge profile of a sequence would assist in the functional interpretation of IDPs and IDRs. PhosIDP is a web tool that shows variation of charge and fold propensity upon phosphorylation. In combination with the displayed location of protein domains, the information provided by the web tool can lead to functional inferences for the consequences of phosphorylation. IDRs are components of many proteins that form biological condensates. It is shown that IDR charge, and its modulation by phosphorylation, is more tightly controlled for proteins that are essential for condensate formation than for those present in condensates but inessential.
电荷是决定无规卷曲蛋白质（IDP）和无规卷曲区域（IDR）性质的关键因素。IDP 和 IDR 富含磷酸化位点，磷酸化会改变电荷。可视化磷酸化在多大程度上调节序列的电荷分布，将有助于 IDP 和 IDR 的功能解释。PhosIDP 是一种网络工具，可显示磷酸化对电荷和折叠倾向的影响。结合显示的蛋白质结构域位置，网络工具提供的信息可以对磷酸化的后果进行功能推断。IDR 是许多形成生物凝聚物的蛋白质的组成部分。结果表明，对于对于凝聚物形成所必需的蛋白质，其 IDR 电荷及其磷酸化调节比凝聚物中存在但非必需的蛋白质更为严格。
