Answer :
Final answer:
Polar amino acids interact with water on the surface of soluble proteins, while hydrophobic amino acids are sequestered in the protein's interior.
Explanation:
Polar and charged amino acid residues tend to be found on the surface of soluble proteins, allowing them to interact with water, while nonpolar amino acids are typically found in the interior of the protein to avoid water contact. In membrane proteins, hydrophobic amino acids are located where they can associate with the hydrophobic tails of phospholipids, while polar and charged amino acids interact with the polar head groups or the aqueous solution.
Learn more about Protein Folding and Amino Acids here:
https://brainly.com/question/45953718