Fig. 3

In silico analysis of the AB_hRXRB sequence. A Analysis of the amino acid composition using the Composition Profiler. The plot illustrates the enrichment (values above zero) and depletion (values below zero) of given amino acid residues relative to the proteins from the SwissProt and Disprot 3.4 (dataset with disordered proteins) databases. The amino acid residues are arranged from the most order-promoting to the most disorder-promoting potential. B Uversky plot [46] of the mean hydropathy versus mean absolute net charge of 105 completely ordered proteins (open squares) and 54 completely disordered proteins (gray circles). The solid line represents the border between the ordered and disordered proteins. The magenta diamond corresponds to AB_hRXRB. C. The prediction of the degree of disorder in the AB_hRXRB sequence calculated from the primary structure. Two algorithms were used – IUPRED2 (short) [44, 45] and PONDR (VLXT) [46]. A score above 0.5 indicates a high probability of disorder. D. Protein backbone dynamics predicted with DynaMine [47, 48]. An S2 value larger than 0.8 indicates high rigidity of the protein backbone, whereas an S2 value lower than 0.69 indicates high flexibility, which is typical for disordered segments. Values between 0.69 and 0.8 are characteristic of the context-dependent structural organization of polypeptide chains