Fig. 1
From: Does one plus one always equal two? Structural differences between nesfatin-1, -2, and nesfatin-1/2
Proteolytical processing and potential intrinsic disorder regions of human nesfatins. (A) Schematic representation of the hNucb2 structure and products of its proteolytical processing. (B) Charge-hydropathy analysis. The dark gray circles represent the set of 105 completely ordered proteins, and the light gray circles represent the set of 54 completely disordered proteins. The stars represent hN1 (black), hN2 (red) and hN1/2 (blue) proteins. The solid black line is a boundary between the ordered and the unordered region. (C) Prediction of hN1/2, (E) hN1 and hN2 IDRs with the PONDR algorithm. Scores ≥ 0.5 indicate putative disordered regions. (D) The flexibility of the hN1/2, (F) hN1 and hN2 backbones calculated with the DynaMine algorithm. The S2 parameter is a measure of the N–H bond rotational freedom. Below the 0.69 threshold, the region is predicted to be flexible, and above the 0.8 value, the residues are predicted to be rigid. The zone between those thresholds is context dependent