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NCERT Exemplar · Q30

Q.α\alpha-Helix is a secondary structure of proteins formed by twisting of polypeptide chain into right handed screw like structures. Which type of interactions are responsible for making the α\alpha-helix structure stable?

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The α\alpha-helix is stabilized primarily by intramolecular hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of the amino acid four residues ahead, forming a regular helical pattern.

The α\alpha-helix is one of the most elegant examples of how a long, floppy polypeptide chain can fold into a precise, repeating shape. The key question is: what holds this spiral together? It’s not covalent bonds between side chains — those come later in tertiary structure. Instead, the stability of the α\alpha-helix comes from a very specific pattern of hydrogen bonds that form within the backbone itself.

Let’s break down why hydrogen bonding is the correct answer, and why other interactions (like disulfide bonds or hydrophobic forces) are not the primary stabilizers here.

  1. The backbone has built-in hydrogen bond donors and acceptors. Every amino acid in a polypeptide chain has a carbonyl group (C=O\ce{C=O}) and an amide group (N−H\ce{N-H}) in its backbone. In an unfolded chain, these groups are free to hydrogen bond with water. But in the α\alpha-helix, they pair with each other instead.

  2. The hydrogen bonding pattern is regular and predictable. In a right-handed α\alpha-helix, the carbonyl oxygen of residue nn forms a hydrogen bond with the amide hydrogen of residue n+4n+4. This means every turn of the helix (about 3.6 amino acids) is locked in place by these bonds. The bonds run parallel to the helix axis and are nearly linear, which makes them strong.

  3. These are intramolecular, not intermolecular, bonds. The hydrogen bonds form within the same polypeptide chain, not between different chains. This is what distinguishes secondary structure from quaternary structure.

  4. Why not other interactions?

    • Disulfide bonds (−S−SX−\ce{-S-S-}) are covalent and form only between cysteine residues — they are rare in α\alpha-helices and not required for helix formation.
    • Hydrophobic interactions and ionic bonds involve side chains and are more important for tertiary folding, not the regular backbone pattern of secondary structure.
    • Van der Waals forces contribute to packing but are not the primary stabilizing force. …

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