Question:

The most common secondary structure of protein molecule is-

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There are 3.6 amino acid residues per turn of a standard alpha helix.
Proline is often called a "helix breaker" because its structure is incompatible with the geometry of a standard alpha helix.
  • Beta helix
  • Gamma helix
  • Alpha helix
  • Delta helix
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The Correct Option is C

Solution and Explanation

Step 1: Understanding the Question:
The question is related to protein biochemistry, specifically looking for the most frequently occurring secondary structural motif in proteins.

Step 2: Detailed Explanation:


Protein Levels of Organization: Proteins have four levels of structure: primary (sequence), secondary (local folding), tertiary (3D shape), and quaternary (multi-subunit).

Secondary Structure: This level refers to the spatial arrangement of the polypeptide backbone, stabilized primarily by hydrogen bonds.

The Alpha Helix ($\alpha$-helix): This structure was first proposed by Linus Pauling.

• In an $\alpha$-helix, the polypeptide chain is wound tightly around an imaginary axis, with the R-groups of the amino acids protruding outward.

• Stability is provided by hydrogen bonds between the carbonyl oxygen (C=O) of one amino acid and the amide hydrogen (N-H) of the amino acid located four residues ahead in the sequence.

Prevalence: The $\alpha$-helix is the most common and thermodynamically stable secondary structure found in many globular and fibrous proteins (like keratin).

• While the beta-pleated sheet is also common, the $\alpha$-helix is generally considered the "default" or most frequent local folding pattern due to its efficient hydrogen bonding network.
Final Answer:
The alpha helix is the most common and fundamental secondary structure found in proteins across various organisms.
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