Finally, we demonstrate that the modifications do not alter the distributions of the dihedral angles in protein simulations. We performed MD simulations of the 1CVO 1 system both with and without the modifications to the torsion potentials of titratable amino acids, with either (i) all these residues protonated, (ii) all deprotonated, or (iii) all Asp residues deprotonated and all other residues protonated. In Figure we plot the distributions of the dihedral angles for which corrections were introduced. The high similarity between the distributions suggests that the corrections do not lead to the sampling of different dihedral distributions, even if the relative weights of the minima are slightly altered, in particular for the H-O-C-O dihedral. We conclude, that the corrections introduced to facilitate sampling of the dihedral and λ-coordinates, do not significantly alter the protein conformational landscape and can hence be used to perform both normal and constant pH MD simulations.