I am studying aromaticity, and apparently, aromaticity is common in biological molecules, just like 6-member rings (relieve ring strain and angle strain). I was wondering: is it because aromaticity makes the compound more stable to prevent unwanted reactions/modifications?
I finally found something interesting. Tyrosine, phenylalanine, and tryptophan interacts with cation-pi interactions in proteins to stabilize secondary structures. They are also over-represented in protein binding sites.