Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a β chain region located in the interior of the protein. In deoxyhemoglobin, however, this pocket is located on the surface of the protein. In deoxyhemoglobin S, Val 6 interacts with this surface pocket, leading to aggregation of HbS. Choose two amino acids that would be reasonable canidates for the pocket-Val 6 interaction.

(A) phenylalanine

(B) leucine

(C) serine

(D) arginine

(E) glutamate

Question

Katelyn Harmon

Biology

14 January, 17:02

Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a β chain region located in the interior of the protein. In deoxyhemoglobin, however, this pocket is located on the surface of the protein. In deoxyhemoglobin S, Val 6 interacts with this surface pocket, leading to aggregation of HbS. Choose two amino acids that would be reasonable canidates for the pocket-Val 6 interaction.

(A) phenylalanine

(B) leucine

(C) serine

(D) arginine

(E) glutamate

+4

Answers (1)

Know the Answer?

Jean · Answer 1

A & B

Explanation:

Leucine and phenylalanine have hydrophobic side chains, which means that they can interact with valine in the pocket. All other aminoacids on the list have polar (two electrically charged) side chains and cannot form hydrophobic pockets.