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BIO NMDCAT Proteins
nmdcat.online June 29, 2026

In sickle cell anemia, a single amino acid substitution in the β-chain of hemoglobin replaces a hydrophilic glutamate with a hydrophobic valine at position six. This change directly affects the protein’s structure by

A. Disrupting a critical disulfide bond in the quaternary structure
B. Introducing a sticky hydrophobic patch on the protein surface that causes polymerization of deoxygenated hemoglobin
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C. Breaking the iron-porphyrin coordination bond in the heme group
D. Causing the complete dissociation of the α and β subunits

📝 Explanation

The Val-6 substitution creates a hydrophobic patch on deoxyhemoglobin, leading to polymerization and sickling of red blood cells.

📖 Additional Information

  • Disrupting a critical disulfide bond in the quaternary structure
  • Introducing a sticky hydrophobic patch on the protein surface that causes polymerization of deoxygenated hemoglobin
  • Breaking the iron-porphyrin coordination bond in the heme group
  • Causing the complete dissociation of the α and β subunits

The Val-6 substitution creates a hydrophobic patch on deoxyhemoglobin, leading to polymerization and sickling of red blood cells.

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