Fig. 2

Distinguishable spatio-temporal coordination dynamics of Cx43 HC-HC model under closed versus open Cys disulfide bond preconditions. A Close view of the interface residues 55N-56T-57Q-58Q during 100 ns MD simulation (top left), top view of residues forming trans-GJ SCs in the last 10 ns MD simulation (top right) and dynamics of trans-GJ SCs (bottom) in the Cx43 HC-HC model in the closed Cys disulfide configurations. B Close view of the interface residues 55N-56T-57Q-58Q during 100 ns MD simulation (top left), top view of residues forming trans-GJ SCs in the last 10 ns MD simulation (top right) and disappearance of trans-GJ SCs (bottom) in the Cx43 HC-HC model in the open Cys disulfide configurations. Residues of trans-GJ SCs 55N-56T-57Q in pre- and post-GJ subunits in A-J, B-I, C-H, D-G, E-L and F-K pairs are highlighted purple, grey, red, brown, green and blue, respectively. Trans-GJ SC pairs are designated as subunit name + residue number + 1-letter residue code. Residue colors: 55N, red: 56T, green: 57Q, cyan: 58Q, black: 59P