Proline is unique due to its cyclic structure, which introduces a sharp kink in the α-helix, disrupting its regular helical conformation. The nitrogen atom in proline is part of a rigid ring, making rotation around the N-C bond impossible. Additionally, proline lacks a hydrogen atom on its nitrogen to participate in backbone hydrogen bonding, which is essential for α-helix stability.
| List I (Enzyme) | List II (Function) |
|---|---|
| (A) Cytochrome oxidase | (I) Electron transport system |
| (B) Topoisomerases | (II) Change linking number |
| (C) Cohesins | (III) DNA Replication |
| (D) PCNA | (IV) Cell cycle |
| List I (Enzyme) | List II (Function) |
|---|---|
| (A) Cytochrome oxidase | (I) Electron transport system |
| (B) Topoisomerases | (II) Change linking number |
| (C) Cohesins | (III) DNA Replication |
| (D) PCNA | (IV) Cell cycle |
| List I (Vitamin) | List II (Disorder) |
|---|---|
| (A) Vitamin-A | (I) Night blindness |
| (B) Vitamin-D | (II) Scurvy |
| (C) Vitamin-C | (III) Fat-soluble vitamin |
| (D) Vitamin-K | (IV) Blood clotting |