The figure below shows amino acid interactions between the a /B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 a, R141 a, D126 a, K127 Noncovalent

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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The figure below shows amino acid interactions between the a /B2 subunit interface of hemoglobin.
These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in
the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most?
Include both the residue and the residue number in your response (For example, V1 or K127).
B, V34
a, R141
a, D126
a, K127
Noncovalent
Transcribed Image Text:The figure below shows amino acid interactions between the a /B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 a, R141 a, D126 a, K127 Noncovalent
Expert Solution
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Hemoglobin is a tetrameric protein in solution, composed of two alpha and two beta subunits. Due to change in the pH of surrounding environment (accumulation of CO2 in the tissues), protonate some residues present at the interface of alpha and beta subunits. The protonation of specific residues change the conformation of hemoglobin into the T-state. T-state conformation of hemoglobin has low affinity for O2. Affinity of O2 can be defined by the Kd value, higher Kd value means low affinity and low Kd value means high affinity.  

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