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nmdcat.online June 27, 2026

In the tertiary structure of a water-soluble globular protein, amino acids with non-polar, hydrophobic R-groups are most likely to be found

A. On the protein's surface, interacting with water
B. Buried in the protein's interior, away from water
✓
C. Evenly distributed throughout the protein
D. Only at the N-terminal end of the polypeptide chain

📝 Explanation

During protein folding, hydrophobic R-groups tend to cluster in the protein's interior to avoid contact with the aqueous cellular environment (hydrophobic effect). Conversely, hydrophilic and charged R-groups are typically positioned on the surface where they can interact with water.

📖 Additional Information

  • On the protein's surface, interacting with water
  • Buried in the protein's interior, away from water
  • Evenly distributed throughout the protein
  • Only at the N-terminal end of the polypeptide chain

During protein folding, hydrophobic R-groups tend to cluster in the protein's interior to avoid contact with the aqueous cellular environment (hydrophobic effect). Conversely, hydrophilic and charged R-groups are typically positioned on the surface where they can interact with water.

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