Please answer Biochemistry questions 1-8 on the sheets attached in photos. Thank

Question

Please answer Biochemistry questions 1-8 on the sheets attached in photos. Thank you Please answer Biochemistry questions 1-8 on the sheets attached in photos. Thank you Pape 1 of 2 I) The saturation curves for two myoglobin mutants are shown below. (4 pts total) 100 90 80 70 60 50 40 30 20 10 a) Estimate the K, values for both mutants. (Refer to your notes for the interpretation of K, with respect to binding curves,) (2 pts) b) Based on the K, values which mutant binds oxygen more tightly? (2 pts) % saturaton (mutant 1) % saturaton (mutant 2 0 20 40 60 80 100 pO2 (torr) 2) In class, we discussed the binding curve of oxygen to hemoglobin. If oxygen bound with complete cooperativity, the Hill coefficient would be 4. On the other hand, if the binding of each oxygen were completely independent of each other, the Hill coefficient would be I (identical to myoglobin). (4 pts total) a) What can we say about the binding of oxygen to hemoglobin given that the Hill coefficient is 2.8 (2 pts) b) Use LeChatelier's Principle and the linked equilibria we discussed in class to explain the cooperative nature of oxygen binding to hemoglobin. (2 pts) 3) In class, we discussed three other allosteric effectors of hemoglobin: hydronium (H); carbon dioxide; and 2,3-bisphosphoglycerate (BPG). Refer to your notes to answer the following... .&8pts total) a) write the relevant equilibrium (or equilibria) for each effector (4 pts); b) bricly describe how each effector reduces hemoglobin's affinity for oxygen (4 pts) 4) Mutations are attributed to function (or loss of function) in fetal hemoglobin and sickle-cell anemia. (4 pts total) a) What mutation distinguishes fetal hemoglobin from adult hemoglobin? How does this affect fetal hemoglobin's affinity for oxygen in the presence of BPG? (2 pts) b) What mutation is present in sickle-cell hemoglobin? How does this cause anemia? (2 pts)

Explanation / Answer

Question 1

Higher the initial slope of the % saturation curve, lower is the value of the binding constant K_D.

Thus, observing the given plot, K_D value of mutant 2 is higher than that of mutant 1.

Thus, mutant 2 binds oxygen more tightly.

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