Glycans coat the surface of all cells on Earth, serving as protection and identification to other cells and macromolecules. Glycan-binding proteins, including lectins, engage specific carbohydrate residues on these glycans to activate downstream functions. The proteins distinguish structurally similar monosaccharides within glycans through non-covalent binding interactions. However, saccharides, unlike other small molecule ligands, are largely hydrophilic, and as a result, often form weak, micromolar interactions with proteins. Carbohydrate-binding proteins rely on binding motifs that involve three key intermolecular interaction types: hydrogen bonding, metal-ion bridges, and carbohydrate-aromatic interactions. While the first two are relatively well understood, there is no consensus on the energetic favorability of carbohydratearomatic interactions nor the relationship between their orientation and energetics. Thus, modeling carbohydrate-aromatic interactions is essential to understanding their role in enabling selective recognition. Doing so will increase our understanding of protein-glycan interactions in biology and assist in the development of glycomimetic therapeutics.