. In the experiments of Barrick, et al. ( observed that replacement of histidine by a noncovalently bonded imidazole not only reduced cooperativity but also increased the oxy- gen affinity of the hemoglobin. Suggest an explanation. it was
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- Which 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 environmentsHemoglobin exhibits positive cooperativity. What is positive cooperativity? Explain how hemoglobin exhibits this property.Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?
- A patient of African American decent came in due to vasooclusive symptoms, you suspect a condition that causes polymerization of the mutant hemoglobin upon deoxygenation in the tissues. a. What conditions can facilitate polymerization? b. Explain the effects of metabolic acidosis to facilitate polymerization?Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.Correlate the conformational changes to the cooperative behavior of the oxygen-binding ability of hemoglobin
- Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?“The binding of oxygen to hemoglobin exhibits positive cooperativity.” Explain brieflyThe number of high-affinity binding sites in the T form of hemoglobin is _______The number of low-affinity binding sites in the T form of hemoglobin is _______
- You are studying with a friend who is describing the Bohr effect. She tells you that in the lungs, hemoglobin binds oxygen and releases hydrogen ion; as a result, the pH increases. She goes on to say that in actively metabolizing muscle tissue, hemoglobin releases oxygen and binds hydrogen ion and, as a result, the pH decreases. Do you agree with her reasoning? Why or why not?People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major reason for this structural change is mutation of glutamic acid to valine. This leads to a Exposure of polar amino acids, leading to disintegration of hemoglobin. b Burying of polar amino acids, leading to disintegration of hemoglobin. c Exposure of non-polar amino acids leading to long fiber formation. d Burying of non-polar amino acids thereby increasing hydrophobic interactions and formation of long fibres.Inhibin and activin are similar molecules; however they have very different physiological roles. Discuss these differences.