Proteins are found to have two different types of secondary structures via α-helix and β-pleated sheet structure. The α-helix structure of a protein is stabilized by-

1. Peptide bonds

2. Van der waals forces

3. Hydrogen bonds

4. Dipole-dipole interactions

 

Hint: Each hydrogen in -NH group of each amino acid bonded to the oxygen atom of C=O of an adjacent turn of the helix 

 Secondary structures of protein denote the shape in which a long polypeptide chain exists. The secondary structure exists in two types of structure α - helix and β - pleated sheet structure.

In α - helix structure, a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw with -NH group of each amino acid rest hydrogen-bonded to > = 0 of adjacent amino acid, which form a helix.