Fig. 3

The structure of open solo HC model may be better represented by open Cys disulfide bonds. A RMSD changes of the extracellular region compared to the initial structure (left) and number of specific H-bonds between Cys residues during the 100 ns MD (right) in the Cx43 GJC model. B RMSD changes of the extracellular region compared to the initial structure (left) and number of specific H-bonds between Cys residues during the 100 ns MD (right) in the Cx43 HC model. C RMSD changes of the extracellular region compared to the initial structure (left) and number of specific H-bonds between Cys residues during the 100 ns MD (right) in the Cx43 HC-HC model. In order to compare HC model with GJC and HC-HC models, only the number of H-bonds on the A-F subunits were counted. Theoretically, two H-bonds can be formed on each subunit since Cys residues can be either proton donors or acceptors, totaling a dozen of H-bonds between Cys residues on all subunits. D Extracellular view of the EL1 (left) and EL2 (right) regions of the A-F subunits of the Cx43 GJC (red), Cx43 HC (green) and Cx43 HC-HC (brown) models with open Cys disulfide bond at the end of the100 ns MD runs. Extracellular loops are shown in cartoon representation, interface residues (55–58 and 194–196) are shown in stick