A protein’s structure is determined by its amino acid sequence and post-translational modifications, and provides the basis for its physiological functions. Across all organisms, roughly a third of the proteome comprises proteins that contain highly unstructured or intrinsically disordered regions. Proteins comprising or containing extensive unstructured regions are referred to as intrinsically disordered proteins (IDPs). IDPs are believed to participate in complex physiological processes through refolding of IDP regions, dependent on their binding to a diverse array of potential protein partners. They thus play critical roles in the assembly and function of protein complexes. Recent advances in experimental and computational analyses predicted multiple interacting partners for the disordered regions of proteins, implying critical roles in signal transduction and regulation of biological processes. Numerous disordered proteins are sequestered into aggregates in neurodegenerative diseases such as Alzheimer’s disease (AD) where they are enriched even in serum, making them good candidates for serum biomarkers to enable early detection of AD.

蛋白质的结构由其氨基酸序列和翻译后修饰决定，并为其生理功能提供基础。在所有生物体中，大约三分之一的蛋白质组包含含有高度非结构化或本质上无序区域的蛋白质。包含或含有大量非结构化区域的蛋白质称为内在无序蛋白质 (IDP)。IDP 被认为通过 IDP 区域的重新折叠参与复杂的生理过程，这取决于它们与多种潜在蛋白质伙伴的结合。因此，它们在蛋白质复合物的组装和功能中起关键作用。实验和计算分析的最新进展预测了蛋白质无序区域的多个相互作用伙伴，暗示在信号转导和生物过程调节中的关键作用。在阿尔茨海默病 (AD) 等神经退行性疾病中，许多无序蛋白质被隔离成聚集体，它们甚至在血清中富集，使其成为血清生物标志物的良好候选者，从而能够早期检测 AD。