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Question

What are the two types of beta sheets?


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Solution

  1. Proteins can either be fibrous or globular based on their shape.
  2. The structure of globular proteins is in 4 levels: primary, secondary, tertiary and quarternary.
  3. The secondary structure of proteins refers to the shape in which a long polypeptide chain can exist. The shapes are of two types: α-helix and β-pleated sheets.
  4. β-pleated sheets consist of β-strands which are polypeptide chains (3 to 10 amino acids long) stretched out to almost maximum extension. They are laid side-by-side and bonded by hydrogen bonds existing between the C=O and -NH- groups of adjacent polypeptide chains. Adjacent β-strands can form hydrogen bonds in either parallel, antiparallel or mixed arrangements.
  5. In the antiparallel arrangement, the β-strands are aligned such that the C=O groups of one strand are adjacent to those of the next strand and -NH- groups of one strand are adjacent to those of the next strand. The inter-strand hydrogen bonds are planar in this arrangement which makes this arrangement more stable. The antiparallel arrangement is shown below.

6. In the parallel arrangement, the -NH- groups of adjacent strands are aligned and the inter-strand hydrogen bonding is non-planar. This makes the parallel arrangement less stable. The parallel arrangement is shown below.

7. Thus, β-sheets can have hydrogen bonding between the adjacent strands in a parallel or antiparallel arrangement.


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