Dosztányi Zsuzsanna, Csizmok Veronika, Tompa Peter, Simon István
Institute of Enzymology, BRC, Hungarian Academy of Sciences, PO Box 7, H-1518 Budapest, Hungary.
Bioinformatics. 2005 Aug 15;21(16):3433-4. doi: 10.1093/bioinformatics/bti541. Epub 2005 Jun 14.
Intrinsically unstructured/disordered proteins and domains (IUPs) lack a well-defined three-dimensional structure under native conditions. The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing interresidue interactions. Optional to the prediction are built-in parameter sets optimized for predicting short or long disordered regions and structured domains.
内在无序蛋白和结构域（IUPs）在天然条件下缺乏明确的三维结构。IUPred服务器提出了一种新算法，通过估计氨基酸序列的总残基间相互作用能来预测这些区域，其假设是IUP序列由于无法形成足够的稳定残基间相互作用而不能折叠。预测可选择为预测短或长的无序区域和结构化结构域而优化的内置参数集。
