α-helix conformation?
(D) Ala-Arg
Ala-Arg shows the highest propensity for α-helix conformation among the given pairs due to their favorable individual helix-forming tendencies. The correct answer is (D) Ala-Arg, key for protein folding in exams like NEET/JEE biotech.
Correct Answer
(D) Ala-Arg.
Alanine (Ala) has the highest α-helix propensity (strong helix former, ΔG ≈ 0 kcal/mol), while Arginine (Arg) is favorable (≈0.21 kcal/mol). Their combination supports stable H-bonding and minimal backbone entropy loss in helices.
Alpha Helix Basics
α-Helices form via backbone H-bonds (i to i+4 residues). Propensity depends on side-chain steric effects, H-bonding, and entropy: Ala excels due to small methyl group; helix breakers like Pro/Gly disrupt via rigidity/flexibility.
Option Breakdown
(A) Gly-Asp
Incorrect. Glycine (Gly, lowest propensity ≈1 kcal/mol worse than Ala) is a helix breaker due to high conformational flexibility. Asp has moderate propensity but can’t compensate Gly’s entropy penalty.
(B) Pro-His
Incorrect. Proline (Pro) is the strongest helix breaker (no backbone amide H-bond donor, rigid ring). His is neutral/moderate; Pro dominates, preventing helix initiation/continuation.
(C) Gly-Pro
Incorrect. Worst pair: Gly’s flexibility + Pro’s rigidity sterically clash and disrupt H-bonding network entirely. Common in turns, not helices.
(D) Ala-Arg
Correct. Ala (top propensity) pairs with Arg (good helix former via guanidinium H-bonding/salt bridges). High combined stability in solvent-exposed helices.
Propensity Ranking Table
| Amino Acid | Helix Propensity (kcal/mol relative to Ala) | Role |
|---|---|---|
| Ala | 0 (highest) | Strong former |
| Arg | 0.21 | Favorable |
| Gly | ~1.0 (lowest) | Breaker |
| Pro | >1.5 | Strong breaker |
| Asp/His | 0.4-0.5 | Moderate |


