Our analysis of non-covalent protein-carbohydrate binding interactions in the PDB reveals critical attributes of CH-p interactions between b-D-galactose and tryptophan, tyrosine, and phenylalanine residues. We found that the single amino acid-carbohydrate interaction energies are energetically favorable by 4 to 8 kcal/mol (i.e., more than hydrogen bonding interactions formed by those same pairs), demonstrating the importance of CH-p stacking interactions in proteincarbohydrate binding. The strongest interactions were formed with tryptophan, while those formed with tyrosine and phenylalanine were generally weaker. This effect is predominantly driven by the size and electronics of the aromatic ring system, with larger rings and those with higher electron density enabling more favorable CH-p contacts.