With these replicas in hand, we obtained important insights regarding the interactions between the tetramerization domain of p53 and Tat, with particular emphasis on the binding regions in both proteins. In the research conducted by Gabizon and colleagues, two specific domains within the Tat protein were suggested as directly involved in complexation: Tat(47-57) also known as the basic patch and Tat(1-31) . These regions exhibit contrasting amino acid compositions. As such, Tat(47-57), characterized by a high abundance of lysine and arginine residues, exhibits a net charge of +8, whereas Tat(1-31), primarily composed of cysteine residues and a hydrophobic core, carries a total charge of only +2. For the tetramerization domain of p53, residues 326-355 have been identified as the specific domain directly engaging with Tat. In their investigation, Gabizon and colleagues noted that the initial interaction between these two proteins entails long-range electrostatic interactions, thereby corroborating the involvement of highly charged Tat(47-57) domain in the binding process. Later, this initial interaction is fine-tuned by some additional ones with lower ionic character, implying that Tat(1-31) becomes the main region in Tat to interact with p53 (for further details, the reader should refer to the original paper). As for the tetramerization domain of p53, the researchers reported that the binding region in p53 spans residues Glu326 to Arg342.