Together with hydrogen bonding, hydrophobic interactions and ion pairing, vdW dispersion is one of the main driving forces for protein folding . Our results underscore the importance of vdW dispersion and enable better understanding of regions that are responsible for intraprotein interactions. Our model can also treat interaction with solvent and charges, which are inherent for some amino-acids (Asp, Glu, Lys, Arg) and surrounding ions. Electric fields from these charges can amplify dispersion interactions in amino-acids by up to 35% . The relative importance of electric-field driven vdW effects in proteins needs further assessment, however, it might compete with salt bridges and cation-π interactions.