Proteins are complex biological molecules that perform a wide variety of functions within living organisms. One common secondary structure found in proteins is the \(\alpha\)-helix. The stabilization of this structure is crucial for the protein’s functionality and is primarily due to a specific type of interaction.
The \(\alpha\)-helix is a right-handed coil structure. The key factor stabilizing this structure is the hydrogen bonds that form between the backbone atoms of the polypeptide chain.
To understand why other options are not correct:
Therefore, the correct answer is that hydrogen bonding is responsible for the stabilization of the \(\alpha\)-helix structure in proteins.
| Bond Type | Relation to \(\alpha\)-Helix Stabilization |
|---|---|
| Ionic Bonding | Not involved in \(\alpha\)-helix stabilization |
| Hydrogen Bonding | Primary force stabilizing the \(\alpha\)-helix |
| Covalent Bonding | Does not stabilize \(\alpha\)-helix directly |
| Van der Waals Forces | Contributes to overall stability, but not primarily |
What is the difference between native protein and denatured protein?



An essential part of every cell in our body, protein is one of the three macronutrients which is required by our body in larger amounts. Proteins are made up of linear chains of smaller units called amino acids. Every biochemical process that takes place inside our bodies is possible because of these proteins. Proteins are 3-dimensional structures that are assembled with different amino acid sequences.
Proteins are used in many ways. Some of their functions are:
Proteins are classified on the basis of:
A protein molecule is made from a long chain of amino acids, each linked to its neighbor through a covalent peptide bond. The structure of proteins are divided into four types: