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 Ka of hemoglobin for O the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a, D126 a, K127 Noncovalent Interactions

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 Ka of hemoglobin for O the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a, D126 a, K127 Noncovalent Interactions

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 19QP: A person was found to have very low levels of functional beta globin mRNA and therefore very low...

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An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hillcoefficient? Explain your answers.
Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity?
Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity (Please provide clear and sufficient explanation for each part, thank you!)
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