The vdW polarization also impacts chemical densitybased analysis, as shown by the NCI index. Our results highlight how vdW polarization enhances the visualization of noncovalent interaction regions, and requires a revision of our understanding of NCI surfaces. The Fip35-WW protein example illustrates that long-range vdW interactions are crucial for understanding protein folding, and thus vdW-induced density shifts are essential. Furthermore, vdW polarization may trigger higherorder interactions, both within proteins and with their solvent, via the dipole-correlated Coulomb singles mechanism, contributing up to 6 kJ/mol for S12L-like systems . This effect is expected to increase in proteins due to their delocalized interactions and presence of charged residues . Hence, further exploration of the interplay between dispersion and polarization in complex systems is necessary.