Prediction of Folding Patterns for Intrinsic Disordered Protein

Abstract The conformation flexibility of natural protein brings more complexities in the system, and more difficulties 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 prediction of protein intrinsic disorder, 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 disorder along protein sequence, based on a complete set of folding shapes for five amino acids which is described by 27 of protein folding shape code (PFSC) with digital alphabetical description. The PFVM integrally exhibited the protein intrinsic disorder with disorder regions, degree of disorder as well as folding pattern. The advantage of PFVM will not only provide rich information for IDP and IDR, but also may promote the study of protein folding problem.