Amino acids with hydrophobic R groups are most often found in the interior of folded proteins. true false

True.

Explanation:

Amino acids with nonpolar, hydrophobic R groups combine together inside the protein, thereby making hydrophilic amino acid that is outside to interact with the water molecules that surrond it. The hydrophobic molecules tend to avoid water by coalescing to form an oily or waxy droplet. This then make hydrophobic and amino acids to come together in the interior of proteins, which is far from the aqueous environment.