DescriptionThe study of DNA-protein interactions is important since these associations are critical to the operation of living cells. DNA-protein contacts show distinct microenvironments. Hybridization is a notable atomic feature that contributes to the distribution of charge within a protein. In order to study a manageable amount of discreet data, a dataset of 499 non-redundant structures was generated. These structures were chosen from DNA-protein structures of high resolution (> 2.5วบ), available in the Protein Data Bank up to June 2011. This research describes differences in DNA-protein interactions based upon atomic hybridization within the set of non-redundant protein structures generated. Although generalizations can be made in terms of hybridization-dependent DNA-protein interactions, the data in this research show hydrogen bond donor-acceptor relationships, as well as electrostatic (positive-negative) attractions, are the primary features regulating close contacts in the major grooves. In general, atoms with a more electropositive environment show a greater number of close contacts with sp2 hybridized atoms, and conversely atoms with a more electronegative environment show a greater number close contacts with sp3 hybridized atoms. However, for proteins comprised of amino acids with delocalized electrons, it is the charge (positive or negative) on the functional group, as well as the structure (cyclic or aliphatic) that have the greatest impact on the number and type of close contacts.