An important aspect to consider is whether the exponential relation is unique to dipeptide systems or would fail to emerge for more extensive systems. For this reason, the Alanine tetra-peptide (Ala-Ala-Ala-Ala) was studied as well, see Figure . The choice for this particular tetra-peptide is deliberate as the geometry of the individual Alanine amino acid is less polymeric in itself. We retrieve a similar R 2 score for the tetra-peptide as the dipeptide, pointing out that I paq AB indices should be safely transferable to larger systems. These patterns confirm that quantum correlations weaken exponentially as atomic distance increases. These findings are crucial for understanding the behavior of larger polypeptides, demonstrating that electronic interactions weaken predictably with increasing atomic distances, thereby reinforcing the concept of electronic nearsightedness in complex molecular structures. At this particular point, it is fair to note that all computational results have been obtained at the DFT level of theory. The choice of a computationally inexpensive method has been deliberate for twofold reasons. First, DFT remains the most popular ab initio approach for biomolecular systems, regardless of CCSD(T) recently emerging as a valid competitor for extensive bio-molecular systems . Second, despite the computational scaling, it allowed for the generation of the complete dataset of dipeptide systems that is large enough to capture statistical trends. However, it is crucial to dissect some of the conclusions at a higher level of theory. Because of the readily availability of reliable RDMs within its formalism, the choice fell on DMRG. Two specific dipeptides, Gly-Gly and Ala-Gly, were selected for comparison with the more precise and computationally demanding DMRG calculations. These dipeptides were chosen because they are the smallest, making it feasible to perform DMRG calculations using a full Complete Active Space (CAS) approach based on AOs. We have illustrated only the Gly-Gly result, as the result is closely comparable to that of the Ala-Gly dipeptide, however, the Ala-Gly result is presented in Figure in Appendix A.2 for the interested reader.