Abstract
In order to analyze the interaction between proteins, smoothed atomic fractal dimension (SAFD) score which was defined by Petit and Bowie for each atom of a protein was mapped on to the protein surface and visualized. This method was applied to about forty protein dimers (or DNA and protein). It was found that the interaction sites of proteins tend to include regions with relatively large SAFD, especially for heterodimers and spherical-shaped proteins with contact area less than around 2000Å2.
