1
Question
Proteins are found to have two different types of secondary structures viz. α−helix and β−pleated sheet structure. α−helix structure of protein is stabilised by:
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Solution
Analysing the options
Option-(A):
Peptide bonds are present between the amino acids.
Option-(B):
Other interactions like van der Waals forces or dipole-dipole interactions do not help in the stabilization of α−helix structure of protein.
Option-(C):
Proteins are found to have two different types of secondary structures viz. α−helix and β−pleated sheet structure. The α−helix structure of protein is stabilized by hydrogen bonds. These hydrogen bonds are formed between the −NH group of an amino acid residue to the C=O group of another amino acid residue.
So, the correct answer is option (C).
Option-(A):
Peptide bonds are present between the amino acids.
Option-(B):
Other interactions like van der Waals forces or dipole-dipole interactions do not help in the stabilization of α−helix structure of protein.
Option-(C):
Proteins are found to have two different types of secondary structures viz. α−helix and β−pleated sheet structure. The α−helix structure of protein is stabilized by hydrogen bonds. These hydrogen bonds are formed between the −NH group of an amino acid residue to the C=O group of another amino acid residue.
So, the correct answer is option (C).
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