write the mechanism for the reaction of CO2 and the amino terminal of the alpha-1 chain of hemoglobin
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- 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!)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?How does the difference between the-chain and the -chain of hemoglobin explain the differences inoxygen binding between Hb A and Hb F?
- 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 (A)oxygen affinity, (B)the Bohr effect, and (C)the Hillcoefficient? Explain your answers.Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?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 Hill coefficient
- 2,3-Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobins.b. Are the mildly thalassemic individuals with Leporehemoglobin homozygotes or heterozygotes for theunusual allele?c. Why might these mildly thalassemic people produce less Lepore hemoglobin than normal adulthemoglobin?
- Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobinsAmino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.The T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.