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The function of the histidine residue at the C-terminal end of the beta subunits of hemoglobin (called His-HC3), as proposed by Max Perutz, was discussed in class. Suppose that this His residue were mutated to alanine (Ala). That is the only change in the hemoglobin protein structure. Recall that the Ala side chain is a methyl group (-CH3). i) What would you predict would be the effect of the mutation on hemoglobin's binding affinity for O2, at low O2 pressure (pO2)? ii) What would you predict would be the effect of the mutation on binding affinity for O2, at high

The function of the histidine residue at the C-terminal end of the beta subunits of hemoglobin (called His-HC3), as proposed by Max Perutz, was discussed in class. Suppose that this His residue were mutated to alanine (Ala). That is the only change in the hemoglobin protein structure. Recall that the Ala side chain is a methyl group (-CH3). i) What would you predict would be the effect of the mutation on hemoglobin's binding affinity for O2, at low O2 pressure (pO2)? ii) What would you predict would be the effect of the mutation on binding affinity for O2, at high

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
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The function of the histidine residue at the C-terminal end of the beta subunits of hemoglobin (called His-HC3), as proposed by Max Perutz, was discussed in class. Suppose that this His residue were mutated to alanine (Ala). That is the only change in the hemoglobin protein structure. Recall that the Ala side chain is a methyl group (-CH3). i) What would you predict would be the effect of the mutation on hemoglobin's binding affinity for O2, at low O2 pressure (pO2)? ii) What would you predict would be the effect of the mutation on binding affinity for O2, at high O2 pressure? Explain briefly how you decided, for both conditions.
Transcribed Image Text:The function of the histidine residue at the C-terminal end of the beta subunits of hemoglobin (called His-HC3), as proposed by Max Perutz, was discussed in class. Suppose that this His residue were mutated to alanine (Ala). That is the only change in the hemoglobin protein structure. Recall that the Ala side chain is a methyl group (-CH3). i) What would you predict would be the effect of the mutation on hemoglobin's binding affinity for O2, at low O2 pressure (pO2)? ii) What would you predict would be the effect of the mutation on binding affinity for O2, at high O2 pressure? Explain briefly how you decided, for both conditions.
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