ok, so it's just so that they hydrophobic residues are as far away from the water as possible.
the simplest explanation (which is entirely correct, it's not an oversimplification or anything, and it's as deep as you'll need on the mcat and really, for any purpose except physical chemistry) is that the hydrophilic residues group to the outside so that they can interact with the aqueous environment. water does not penetrate deeply beyond the surface of the protein, so this is a convenient place for hydrophobic molecules to locate since they are reasonably shielded from the water. that's really all there is to it. it's the same way micelles work with fatty acids. the polar carboxyl groups orient to the outside of the micelle while the hydrophobic alkyl chains orient towards the inside of the micelle.
that's why valine, which just has an isopropyl group for its R group, generally is found in the interior of the protein.
so just remember, inside is hydrophobic because there's very little water in the inside of the protein, whereas there's a ton of water on the surface (since it's dissolved in water) so hydrophilic residues will be more common on the surface