10.) How would the p 50 of hemoglobin be affected when the partial pressure of CO_2 increases from 20 to 30 torr. 11.) How is the majority of CO_2 generated by respiring tissue transported to back to the lungs? 12.) How does hemoglobin carry CO_2 from the tissues back to the lungs? would this mutation have on the oxygen affinity of Hb Kansas? 14.) Hb Yakima, 99(G1) β Asp → His, disrupts a hydrogen bond that stabilizes the T-state. What affect would this mutation have on the oxygen affinity of Hb Yakima? cysteine of the β-subunit that stabilizes the R-state. How would this mutation affect the oxygen affinity and hill coefficient of Hb Rainier? would this mutation affect the oxygen affinity and allosteric regulation of Hb Cowtown? 17.) ( 3 pts) A toddler has developed abnormal blue skin and blue lips and his blood has turned chocolate brown in color. This condition is called cyanosis and is an inherited hemoglobinopathy. List 3 hemoglobinopathies that would cause the clinical symptoms and explain why the blood is chocolate and the skin is bluish.
Added by Thomas E.
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Therefore p50 increases (it takes higher PO2 to half-saturate Hb). Show more…
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25.) (3 pts) Hb Rainier, 145(HC2) β Tyr → Cys. The mutant cysteine forms a disulfide bond with another cysteine of the β-subunit that stabilizes the R-state. How would this mutation affect the oxygen affinity? (A) increase (B) decrease (C) remain the same (D) cannot be determined. 26.) (3 pts) Hb Rainier, 145(HC2) β Tyr → Cys. The mutant cysteine forms a disulfide bond with another cysteine of the β-subunit that stabilizes the R-state. How would this mutation affect the hill coefficient of Hb Rainier? (A) increase (B) decrease (C) remain the same (D) cannot be determined. 27.) (3 pts) What is the role of His-146 of the β-subunits? 28.) (3 pts) Hb Cowtown, 146(HC3) β His → Leu. What is the role of His-146 of the β-subunits? How would this mutation affect the oxygen affinity of Hb Cowtown? (A) increase (B) decrease (C) remain the same (D) cannot be determined. 29.) (2 pts) A monomeric oxygen-binding protein has a fractional saturation of 0.85 when pO2 = 7.3 torr. What is the value of the hill coefficient n? 30.) (3 pts) A monomeric oxygen-binding protein has a fractional saturation of 0.85 when pO2 = 7.3 torr. What is the value of p50 for this protein? 31.) (2 pts) A monomeric oxygen-binding protein has a fractional saturation of 0.35 when pO2 = 15.8 torr. What is the value of the hill coefficient n? 32.) (3 pts) A monomeric oxygen-binding protein has a fractional saturation of 0.35 when pO2 = 15.8 torr. What is the value of p50 for this protein? 33.) (3 pts) Calculate the fractional saturation of hemoglobin at a pO2 = 15 torr. The Hill coefficient of Hb is 3.0 and using a p50 = 27 torr. 34.) (3 pts) Calculate the fractional saturation of hemoglobin at a pO2 = 15 torr. The Hill coefficient of Hb is 3.0 and using a p50 = 0.30 torr.
Josee P.
More than one thousand hemoglobin (Hb) variants with differing mutations have been identified. Many of these variants are not life-threatening, whereas some, as you know, like sickle cell anemia, can be. The Hb Kempsey variant has one mutation in the beta subunit at position 99, with an asparagine instead of an aspartate. This mutation stabilizes the R state over the T state of Hb, which increases erythropoiesis or red blood cell production. a) Compared to wild-type Hb (one without mutations), how does the affinity of Hb Kempsey change, if at all? b) Show your answer in part (a) by sketching out an oxygen saturation curve for wild-type Hb and Hb Kempsey. c) Will oxygen release into tissues by the Hb Kempsey variant stay the same, increase, or decrease? d) How could you increase the release of oxygen? Explain why. The Hb M-lwate variant has one mutation in both alpha subunits at position 87 (F8) from a histidine to tyrosine. See Figure 15.27 from the text below. F helix Proximal histidine F8 Heme This mutation results in higher levels of methemoglobin and is implicated in cyanosis or blue/purple skin discoloration. Methemoglobin has a different oxidation state than wild-type Hb and can no longer bind oxygen. Assuming that the beta subunits can still bind oxygen, sketch out an oxygen saturation curve for wild-type Hb and Hb M-lwate.
7.a) In hemoglobin Yakima, there is only one mutation Asp + His that disrupts the hydrogen bond that stabilizes the T conformation. Is pS for hemoglobin Yakima higher or lower than that of normal Hb? 6) In hemoglobin Kansas, there is only one mutation Asn102 Thr that disrupts the hydrophobic band that stabilizes the R conformation. Is pSO for hemoglobin Kansas higher or lower than that of normal Hb?
Sri K.
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