Extended Data Fig. 5: Sampling, distributions and dependence on the location within the full-length protein of conformational properties in the pLDDT-based set of IDRs.
From: Conformational ensembles of the human intrinsically disordered proteome
a, Values of the autocorrelation function (ACF) of the Rg for lag times of one (grey), two (red), and three (blue) frames as a function of sequence length. Data are displayed as mean ± s.d. over n = 5 independent simulation replicas. b, S.d. of the apparent Flory scaling exponent, ν, as a function of ν for proteins of different sequence length. c, S.d. of the ratio of the mean-squared end-to-end distance and the mean-squared radius of gyration, \(\langle {R}_{{\rm{ee}}}^{2}\rangle /\langle {R}_{{\rm{g}}}^{2}\rangle \), as a function of \(\langle {R}_{{\rm{ee}}}^{2}\rangle /\langle {R}_{{\rm{g}}}^{2}\rangle \) for proteins of different sequence length. d, S.d. of the conformational entropy per residue, Sconf/N, as a function of Sconf/N for proteins of different sequence length. S.d. values are calculated over n = 5 independent simulation replicas. Dotted lines show the average s.d. e, Correlation between \(\langle {R}_{{\rm{ee}}}^{2}\rangle \) / \(\langle {R}_{{\rm{g}}}^{2}\rangle \) calculated from simulation trajectories and the approximate relation \(\langle {R}_{{\rm{ee}}}^{2}\rangle \) / \(\langle {R}_{{\rm{g}}}^{2}\rangle =(2\nu +1)\times (2\nu +2)\). (ref. 15). f,g, Distributions of (f) \(\langle {R}_{{\rm{ee}}}^{2}\rangle \) / \(\langle {R}_{{\rm{g}}}^{2}\rangle \) and (g) the conformational entropy per residue, Sconf/N, for IDRs in the human proteome; note the logarithmic scale. h–j, Correlation between (h) asphericity, Δ, and ν; (i) prolateness, S, and ν; and (j) Sconf/N and ν. r is the Pearson correlation coefficient. k, Normalized distributions of the absolute difference between ν values, ∣Δν∣, for IDRs from different proteins (grey), within the same protein (blue), and separated by folded domains within the same protein (teal). Vertical bars show mean ± s.e.m. of ∣Δν∣. l,m, Distributions of (l) ν and (m) Sconf/N for IDRs in the different categories of localization within the full-length protein: N-terminal (32.2%), C-terminal (24.8%), between folded domains (15.5%), and IDPs (5.2%). For this analysis we annotated IDRs to be located between folded domains if they are preceded and followed by at least 100 residues which do not overlap with any of the IDRs identified in this work. IDP, fully intrinsically disordered protein.
