Both myoglobin and hemoglobin can adopt both T and R states. Both myoglobin and hemoglobin bind to oxygen with approximately 100% occupancy at normal atmospheric oxygen levels. Each hemoglobin protein can bind 4 BPG molecules, providing a relative destabilization of the R state. CO2 can covalently bind to the N-termini of hemoglobin to stabilize the T state.
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- In one type of hemoglobin mutant the amino acid change generates a strong ionic interaction stabilizing the T state conformation, but only under conditions of lower pH, e.g., at pH 7.2 compared to pH 7.6. Explain what effect this mutation would have on the amount of O2 delivered to the tissue. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the R state in tissues.A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.
- Hemoglobin from different species can have different numbers of subunits. Let's consider three hemoglobin molecules: n = 1, n = 4, and n = 8, where each subunit has an oxygen P50 = 30 torr. (Recall that Pso is essentially a Kp and that oxygen partial pressure (torr) is directly proportional to concentration.) Which molecule transports the most O2 between the lungs (pO2 = 100 torr) and peripheral tissues (pO2 = 30 torr)? Please justify your answer.What is the allosteric effect on O2 binding to the second subunit of hemoglobin after the first subunit binds after O2 binding? to 02? What state would hemoglobin be O A decrease in affinity of hemoglobin for 02: T-State O An increase in affinity of hemoglobin for O2: T-State An increase in affinity of hemoglobin for 02; R-State O A decrease in affinity of hemoglobin for O2; R-StateWhich of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environments
- The amino acid in Hemoglobin that is most found to be most sensitive to pH changes, and hence affects Oxygen binding process around pH 7 is Valine Tyrosine Histidine Aspartic AcidSickle cell anemia is associated with which of the following: Question 27 options: Sticky patches on the hemoglobin surface only present in the T-state Sticky patches on the hemoglobin surface only present in the R-state A mutant form of hemoglobin called Ɣ-hemoglobin Decreased ability to stabilize the T-state with 2,3-bisphosphoglycerate Decreased ability to bind heme because of the Bohr effectAmino 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.
- One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).Allosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformationBPC is a heterotropic allosteric modulator. in which way does this compound change the uptake and release of oxygen in hemoglobin?