Structure of Proteins - Secondary Structure
- Once the primary structure of the protein is formed, it begins to twist into regular patterns that make its secondary structure.
- These twists are formed as a result of the regular pattern of H-bonds.
- There are two types of secondary structures: α-helix and β-pleated sheets.
α-helix:
- It is a rod-like structure.
- Inner portion contains the backbone of the polypeptide and outer portion contains the side chains.
- The helical shape occurs because of the formation of H-bonds between the oxygen atom of the -CO group of one amino acid and the nitrogen atom of the -NH group of the fourth amino acid.
- Thus, the H-bonds are formed every fourth amino acid.
β-pleated sheets:
- In this structure, two linear polymers of amino acids run in opposite direction.
- In this arrangement, the -NH and -C=O groups of an amino acid in one strand form H-bonds with -C=O and -NH groups of the opposing amino acids on the other strand.
Tip: The α-helix and β-pleated sheet structures are found in most globular and fibrous proteins and they play an important structural role.
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There are two types of secondary structures of proteins:
and
sheets.
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