Figure 3

Binding of an IAPP monomer with aLac and Lys. (A) Binding frequencies of IAPP monomers with either aLac or Lys during the course of simulations. (B) Binding probability of each IAPP residue with either aLac or Lys was derived from the IAPP-protein complexes in DMD simulations. Similarly, the binding probabilities of residues in aLac (C) and Lys (D) with IAPP were also computed. The residues with peaks values were highlighted, where the residue indices were re-numbered from 1 in each corresponding sequence. (E) Typical snapshot structures of IAPP-protein complexes. The molecular surfaces of both aLac and Lys were shown to highlight their binding with IAPP (colored grey in cartoon representation), where each protein residue was colored from blue (low) to red (high) according to its binding probability to IAPP as in panels C &D. Two different views were given to illustrate multiple IAPP-binding sites on the protein surfaces, and corresponding electrostatic potential surfaces (estimated with PyMol) were shown in the inset.