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Multiple Choice
Where would the leucine side chain most likely be found in a protein dissolved in water?
A
Exposed on the surface of the protein, interacting with water
B
Coordinating metal ions at the active site
C
Forming hydrogen bonds with water molecules
D
Buried in the interior of the protein, away from water
Verified step by step guidance
1
Understand the chemical properties of leucine: Leucine is a nonpolar, hydrophobic amino acid. Its side chain consists of an aliphatic hydrocarbon group, which does not interact favorably with water.
Recall the structure of proteins in aqueous environments: Proteins dissolved in water typically fold in a way that minimizes the exposure of hydrophobic residues to the surrounding water. Hydrophobic amino acids like leucine are often buried in the interior of the protein.
Consider the role of hydrophobic interactions: Hydrophobic residues cluster together in the protein's interior to avoid contact with water, stabilizing the protein's tertiary structure.
Eliminate incorrect options: Leucine's hydrophobic nature makes it unlikely to be exposed on the surface interacting with water, coordinating metal ions, or forming hydrogen bonds with water molecules.
Conclude the most likely location: Based on its hydrophobic nature, leucine's side chain is most likely buried in the interior of the protein, away from water.