Reducing the torsional barriers without affecting the overall sampling of the conformational space is possible only if the regions near such barriers are sparsely sampled. We, therefore, analyzed the distributions of the dihedral angles in the side chains of titratable amino acids in the publicly available trajectories of G-protein coupled receptors and of SARS-CoV-2 proteins. The distributions of these dihedral angles, plotted in Figure , reflect the shape of the underlying torsion potentials with maxima coinciding with local minima of the potential profiles. The low density near barriers suggests that these barriers are rather high and might be reduced without affecting the dihedral distributions.