Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, Guangdong, China.
Micro Biotech, Ltd., Shanghai, 200123, China.
Sci Rep. 2023 Nov 21;13(1):20343. doi: 10.1038/s41598-023-45969-5.
The conformation flexibility of natural protein causes both complexity and difficulty to understand the relationship between structure and function. The prediction of intrinsically disordered protein primarily is focusing on to disclose the regions with structural flexibility involving relevant biological functions and various diseases. The order of amino acids in protein sequence determines possible conformations, folding flexibility and biological function. Although many methods provided the information of intrinsically disordered protein (IDP), but the results are mainly limited to determine the locations of regions without knowledge of possible folding conformations. Here, the developed protein folding fingerprint adopted the protein folding variation matrix (PFVM) to reveal all possible folding patterns for the intrinsically disordered protein along its sequence. The PFVM integrally exhibited the intrinsically disordered protein with disordering regions, degree of disorder as well as folding pattern. The advantage of PFVM will not only provide rich information for IDP, but also may promote the study of protein folding problem.
天然蛋白质的构象灵活性既增加了其结构与功能关系理解的复杂性，又增加了其难度。无序蛋白质的预测主要集中于揭示涉及相关生物功能和各种疾病的结构灵活性区域。蛋白质序列中氨基酸的顺序决定了可能的构象、折叠灵活性和生物功能。尽管许多方法提供了无序蛋白质（IDP）的信息，但结果主要限于确定没有可能折叠构象知识的区域的位置。在这里，开发的蛋白质折叠指纹采用蛋白质折叠变化矩阵（PFVM）来揭示沿其序列的无序蛋白质的所有可能折叠模式。PFVM 整体展示了无序区域、无序程度以及折叠模式的无序蛋白质。PFVM 的优势不仅为 IDP 提供了丰富的信息，而且可能促进蛋白质折叠问题的研究。
