We recently carried out a study of three diverse peptides (i.e., a lasso peptide, Trpcage, and a small helical protein, mini-CD4) that found charge distributions sampled from ab initio molecular dynamics to be broad. We showed that breadth of charge distributions was associated with significant pairwise coupling of the charges between residues, including those that are distant in both space and sequence. These observations added to a growing body of research that has demonstrated the value of studying these couplings to understand dynamic events in materials , interpret QM/MM simulations , and to guide QM method selection . In this recent work , we quantified both the mutual information and linear cross-correlation of charge distributions and determined that they bore little similarity to the more commonly studied geometric coupling values in these proteins. Nevertheless, one limitation of that study was that the diverse nature of the three proteins did not allow us to determine if small changes in protein sequence could be detected through charge coupling analysis.