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6. Sickle cell anemia is a genetic disease resulting from a single amino acid substitution (glutamate to valine in the sixth position, or E6V) on the surface of the hemoglobin B chain. This mutation causes hemoglobin to polymerize into strands in the deoxygenated state, leading to the erythrocytes forming a sickled shape. a. Speculate as to why the mutation leads to the polymerization of hemoglobin. In the structure below, the red circles show the approximate location of the mutation. a subunits ẞ subunits b. Given that the binding of oxygen to hemoglobin cause the structure of the protein to change, hypothesize why the E6V mutation only causes polymerization in the deoxygenated state.

6. Sickle cell anemia is a genetic disease resulting from a single amino acid substitution (glutamate to valine in the sixth position, or E6V) on the surface of the hemoglobin B chain. This mutation causes hemoglobin to polymerize into strands in the deoxygenated state, leading to the erythrocytes forming a sickled shape. a. Speculate as to why the mutation leads to the polymerization of hemoglobin. In the structure below, the red circles show the approximate location of the mutation. a subunits ẞ subunits b. Given that the binding of oxygen to hemoglobin cause the structure of the protein to change, hypothesize why the E6V mutation only causes polymerization in the deoxygenated state.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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6. Sickle cell anemia is a genetic disease resulting from a single amino acid substitution (glutamate to valine in the sixth position, or E6V) on the surface of the hemoglobin B chain. This mutation causes hemoglobin to polymerize into strands in the deoxygenated state, leading to the erythrocytes forming a sickled shape. a. Speculate as to why the mutation leads to the polymerization of hemoglobin. In the structure below, the red circles show the approximate location of the mutation. a subunits B subunits. b. Given that the binding of oxygen to hemoglobin cause the structure of the protein to change, hypothesize why the E6V mutation only causes polymerization in the deoxygenated state.
Transcribed Image Text:6. Sickle cell anemia is a genetic disease resulting from a single amino acid substitution (glutamate to valine in the sixth position, or E6V) on the surface of the hemoglobin B chain. This mutation causes hemoglobin to polymerize into strands in the deoxygenated state, leading to the erythrocytes forming a sickled shape. a. Speculate as to why the mutation leads to the polymerization of hemoglobin. In the structure below, the red circles show the approximate location of the mutation. a subunits B subunits. b. Given that the binding of oxygen to hemoglobin cause the structure of the protein to change, hypothesize why the E6V mutation only causes polymerization in the deoxygenated state.
Expert Solution
Introduction

The following steps describe the structure of normal and sickle cell hemoglobin and explain the molecular mechanism behind polymerization of hemoglobin in sickle cell anemia as well as discuss the reason for polymerization of sickle cell hemoglobin only in the deoxygenated state. 

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