Fig. 9
From: Design of stable circular permutants of the GroEL chaperone apical domain
A The PONDR® VLXT-based evaluation of the per-residue intrinsic disorder propensity of the ribosomal protein S6 from Thermus thermophiles (UniPrit ID: P23370). The circles denote the position of the sites of the designed breaks in the amino acid sequence. B Dependence of the changes in the global stability (ΔGu) of S6 circular permutants, determined from the analysis of the guanidinium chloride-induced unfolding of the analyzed proteins on the local intrinsic disorder propensity of the designed cleavage cites in the wild type protein. Data were retrieved from Haglund et al. [56] (red circles), Lindberg et al. [58] (pink circles), and Miller et al. [57] (green circles). Pearson correlation coefficient is -0.57, reflecting a moderate negative correlation, which means there is a tendency for high PONDR® VLXT scores to go with low ΔGu values