Most proteins are soluble in the aqueous environment of a cell. Knowing that, where in the overall three-dimensional shape of a protein would you expect to find amino acids with hydrophobic R groups?

Verified step by step guidance

1. Understand the structure of proteins: Proteins are made up of amino acids linked together by peptide bonds forming a polypeptide chain. Each amino acid has a unique side chain, known as an R group, which can be hydrophobic or hydrophilic.
2. Recognize the importance of protein folding: Protein folding is the process by which a protein structure assumes its functional shape or conformation. It is crucial for the protein's function.
3. Identify the role of hydrophobic and hydrophilic R groups: Hydrophobic R groups are typically nonpolar and tend to avoid water, whereas hydrophilic R groups are polar and interact well with water.
4. Predict the location of hydrophobic R groups in a folded protein: Since most proteins function in an aqueous environment inside the cell, the hydrophobic R groups are likely to be tucked away inside the protein structure. This arrangement helps to stabilize the protein structure by keeping these nonpolar groups away from the aqueous environment.
5. Visualize the protein structure: In the three-dimensional structure of a protein, hydrophobic R groups are generally found in the interior of the protein, away from the surrounding water molecules. This helps in maintaining the integrity and functionality of the protein.