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The eukaryotic Cys2His2 zinc finger proteins bind to DNA ubiquitously athighly conserved domains, responsible for gene regulation and the spatialorganization of DNA. To study and understand the zinc finger DNA-proteininteraction, we use the extended ladder in the DNA model proposed by Zhu,Rasmussen, Balatsky \& Bishop (2007) \cite{Zhu-2007}. Considering one singlespinless electron in each nucleotide $\pi$-orbital along a double DNA chain(dDNA), we find a typical pattern for the {\color{black} bottom of the occupiedmolecular orbital (BOMO)}, highest occupied molecular orbital (HOMO) and lowestunoccupied orbital (LUMO) along the binding sites. We specifically looked attwo members of zinc finger protein family: specificity protein 1 (SP1) andearly grown response 1 transcription factors (EGR1). When the valence band isfilled, we find electrons in the purines along the nucleotide sequence,compatible with the electric charges of the binding amino acids in SP1 and EGR1zinc finger.

The Electronic Behavior of Zinc-Finger Protein Binding Sites in the Context of the DNA Extended Ladder Model