Toward the goal of characterizing CH-p interactions in known glycan-binding proteins, a bioinformatic analysis of the Protein Data Bank (PDB), determined that 39% of all protein entries with a carbohydrate contained at least one CH-p stacking interaction formed between the protein and carbohydrate. However, it is worth noting that this analysis included both covalently and non-covalently bound carbohydrates. Because carbohydrates that are covalently bound to the protein have a lower propensity for favorable non-covalent stabilization, this analysis may be a significant underestimate of the frequency of CH-p stacking interactions in non-covalent proteincarbohydrate interactions. Prior computational and experimental analyses have probed the energetic favorability of certain carbohydrate-aromatic interactions. Most NMR evaluations observed that the carbohydrate-aromatic CH-p stacking interaction free energies range from 1-2 kcal/mol, while calorimetry and computational studies of these interactions observe electronic interaction energies ranging from 4-8 kcal/mol. However, all CH-p stacking interactions are not equivalent. The stereochemistry of each carbohydrate informs the orientation of CH bonds and the polarization of these bonds by the neighboring hydroxyl groups. For example, electron-poor C-H bonds should result in more stabilizing CH-π interactions, and hydroxyl group stereochemistry influences the electronics of the glycan C-H bonds. NMR studies have demonstrated that b-Dgalactose forms particularly favorable CH-p stacking interactions with indoles, yet detailed energetics of these interactions and those formed by other amino acid side chains have not been evaluated. Further study is required to determine the energetic favorability of these interactions and the orientational factors that influence their strength.