Difficulty: Easy
Correct Answer: Asp, Ile, and Pro
Explanation:
Introduction / Context:
Amino acids are commonly grouped by their side-chain properties because polarity and charge strongly influence protein folding, enzyme catalysis, and membrane interactions. Typical sets include nonpolar aliphatic (e.g., Ala, Val, Leu), polar/uncharged (e.g., Ser, Thr, Asn, Gln), aromatic (e.g., Phe, Tyr, Trp), acidic (Asp, Glu), and basic (Lys, Arg, His).
Given Data / Assumptions:
Concept / Approach:
Cohesive groupings share similar polarity/charge: nonpolar aliphatics cluster together; basic residues cluster together; aromatics cluster together; mixing acidic with nonpolar residues is not sensible for polarity grouping.
Step-by-Step Solution:
Evaluate Ala, Leu, Val → all nonpolar, aliphatic: sensible.Evaluate Arg, His, Lys → basic/positively charged at physiological pH range: sensible (His is weakly basic but grouped here).Evaluate Phe, Trp, Tyr → aromatic set: sensible despite Tyr’s phenolic OH increasing polarity.Evaluate Asp, Ile, Pro → Asp is acidic/polar negative; Ile is strongly hydrophobic; Pro is nonpolar cyclic imino acid: mixed properties → not a sensible polarity group.
Verification / Alternative check:
Most textbooks and protein parameter tables organize residue properties similarly; hydropathy scales support that Ile/Pro are hydrophobic while Asp is hydrophilic and negatively charged.
Why Other Options Are Wrong:
Common Pitfalls:
Overthinking Tyr’s polarity and assuming it disqualifies the aromatic grouping; forgetting His’s context-dependent charge yet its placement among basics for pedagogy.
Final Answer:
Asp, Ile, and Pro
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