Residue side-chain interactions and backbone conformations altered upon p.G40S mutation. (A) Ribbon model of TM1 and NT in the region of p.G40S. Observer’s perspective is from within the channel pore. The cyan backbone is the initial conformation of the p.G40S monomer. The red transparent structure depicts its deviation during the simulation. Residues of the electrostatic network nearest to position 40 are depicted in the boxed diagrams for WT and p.G40S. (B) DSSP analyses of the residues neighboring G40 in WT simulations and in p.G40S simulations. Intensity of red indicates the number of protomers out of 18 assuming an α-helical conformation (R32 undergoes a significant shift toward α-helix). (C) Differences in electrostatic interaction distances between the N-terminal amide and E41 (first row) and for salt bridges among the electrostatic network (*interprotomeric residue pairs).