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A mutant form of hemoglobin (mt Hb) no longer displays any cooperativity, yet has affinity that is close to that observed with the R-state of Hb. Looking at the Hill Plot below where wild type Hb and wildtype myoglobin wt Mb) are shown, how would you expect mt Hb to look? log (₁-0) 3 2 1 0 -1 Myoglobin nH = 1 -2- Hemoglobin high-affinity state nH = 1 Hemoglobin nH=3 1 0 1 log po₂ Hemoglobin low-affinity state nH=1 L 2 3 It would have a slope of one like wt Mb, but be shifted to the left and display higher affinity matching the high affinity state of Hb It would have a slope of one like wt Mb, but be shifted to the right and display lower affinity matching the low affinity state of Hb It would have a maximal slope of 3, but be shifted to the left like the high affinity state of Hb O It would have a maximal slope of 3, but be shifted to show a p50 value equal to wt Mb

A mutant form of hemoglobin (mt Hb) no longer displays any cooperativity, yet has affinity that is close to that observed with the R-state of Hb. Looking at the Hill Plot below where wild type Hb and wildtype myoglobin wt Mb) are shown, how would you expect mt Hb to look? log (₁-0) 3 2 1 0 -1 Myoglobin nH = 1 -2- Hemoglobin high-affinity state nH = 1 Hemoglobin nH=3 1 0 1 log po₂ Hemoglobin low-affinity state nH=1 L 2 3 It would have a slope of one like wt Mb, but be shifted to the left and display higher affinity matching the high affinity state of Hb It would have a slope of one like wt Mb, but be shifted to the right and display lower affinity matching the low affinity state of Hb It would have a maximal slope of 3, but be shifted to the left like the high affinity state of Hb O It would have a maximal slope of 3, but be shifted to show a p50 value equal to wt Mb

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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A mutant form of hemoglobin (mt Hb) no longer displays any cooperativity, yet has affinity that is close to that observed with the R-state of Hb. Looking at the Hill Plot below where wild type Hb and wildtype myoglobin (wt Mb) are shown, how would you expect mt Hb to look? (¹) 601 3 2 -2 Hemoglobin high-affinity state nH = 1 Myoglobin nμ = Hemoglobin. nH = 3 -1 0 1 log po₂ Hemoglobin low-affinity state nH = 1 L 2 3 It would have a slope of one like wt Mb, but be shifted to the left and display higher affinity matching the high affinity state of Hb It would have a slope of one like wt Mb, but be shifted to the right and display lower affinity matching the low affinity state of Hb It would have a maximal slope of 3, but be shifted to the left like the high affinity state of Hb It would have a maximal slope of 3, but be shifted to show a p50 value equal to wt Mb
Transcribed Image Text:A mutant form of hemoglobin (mt Hb) no longer displays any cooperativity, yet has affinity that is close to that observed with the R-state of Hb. Looking at the Hill Plot below where wild type Hb and wildtype myoglobin (wt Mb) are shown, how would you expect mt Hb to look? (¹) 601 3 2 -2 Hemoglobin high-affinity state nH = 1 Myoglobin nμ = Hemoglobin. nH = 3 -1 0 1 log po₂ Hemoglobin low-affinity state nH = 1 L 2 3 It would have a slope of one like wt Mb, but be shifted to the left and display higher affinity matching the high affinity state of Hb It would have a slope of one like wt Mb, but be shifted to the right and display lower affinity matching the low affinity state of Hb It would have a maximal slope of 3, but be shifted to the left like the high affinity state of Hb It would have a maximal slope of 3, but be shifted to show a p50 value equal to wt Mb
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