# Why are Tyrosine and Tryptophan considered hydrophobic?

Since Tyrosine and Tryptophan are amino acids, their polarity is determined on their side chains or R groups. If their R groups are polar, the amino acid is polar. Both Tyrosine and Tryptophan are listed as non-polar molecules. However, Tryptophan has nitrogen in its side chain and Tyrosine has oxygen, both of which have a high electronegativity compared to the carbon that makes up the bulk of both molecules, which is something commonly seen in polar amino acids like Serine, which has oxygen in its side chain. This should mean that Tyrosine and Tryptophan are polar, so why are they non-polar, even with an electronegative atom in their side chains?

All polar amino acids have either an $$\ce{OH}$$ or $$\ce{NH2}$$ group (when in aqueous environment), and can therefore make hydrogen bonds with other suitable groups.