Electrostatic potential maps: Difference between revisions

It is revealing to visualize the distribution of electrostatic charges, [https://en.wikipedia.org/wiki/Electric_potential electrostatic potential], on molecular [https://en.wikipedia.org/wiki/Van_der_Waals_surface van der Waals surfaces]. Most protein-protein and protein-ligand interactions are largely electrostatic in nature, via hydrogen bonds and ionic interactions. Their strengths are modulated by the nature of the solvent: pure water or high ionic strength aqueous solution<ref>This opening paragraph was adapted from text authored by [[User:Karsten Theis]] in [[Jmol/Electrostatic potential]].</ref>. [[Missing residues and incomplete sidechains|Missing atoms or residues]], nearly universal in [[empirical models]], cause [[Missing_residues_and_incomplete_sidechains#Why_Missing_Residues_Matter|errors in the map]]. Therefore it is '''{{font color|red|crucial to use a model without missing atoms}}''', which could be an [[Missing_residues_and_incomplete_sidechains#AlphaFold_models_have_no_missing_atoms|AlphaFold model]].