Which of the following is incorrect about hemoglobin? a. The binding of O₂ to one subunit decreases the O2-binding affinity of the other subunits Ob. It has two quaternary structures called the T (tense) and the R (relaxed) states c. It displays cooperativity Od. It undergoes conformational changes upon binding 0₂
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- A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?Which of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.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 environments
- The O2-binding curve for Hemoglobin (Hb) is sigmoidal because: a O2 binding to Hb increases the binding affinity of Hb for additional O2. b The pH of blood is near the pKa of histidine. c The pH of the bloodstream changes with changes in O2 concentration. d Hb’s O2-binding affinity changes with changes in pH.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-StateA researcher, in a study involving acid-base properties of RBC's notices the resistance of change in pH, when a small amount of acid or base is added to it. Buffering action of hemoglobin in RBCS is most likely attributed to presence of which of the following factors in the globin chains? Alpha helical structures В Beta pleated sheets C Ferric state of iron D Ferrous state of iron E Histidine residues
- O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohr effect from the molecular perspective. Be sure to include discussion of what causes this (i.e. specific amino acids), why the curves are right shifted with decreasing pH, and why this is logical in delivery of 02 to areas of higher demand. 100 Myoglobin 80- pH 7.6 60 pH 7.4 pll 7.2 40- pH 7.0 pH 6.8 20- Venous 0- 0. 20 10 60 80 Percent saturationOne 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).. 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
- 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 AcidThe graphs below show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (-) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p50 as normal hemoglobin? 1.0- YO, 0.5 0.0 pO,(torr) O A. 1 B. 2 O C. 4 O D. 5 E. Both "2" and "4"Consider the Fe(Il) heme center in hemoglobin. Iron is colored orange and dioxygen is colored red. A. Circle the distal Histidine residue. B. What is the function of the distal Histidine residue? C. What keeps bound oxygen “bent", and not binding orthogonal to the plane of the porphyrin? D. What would happen to Fe(lI) if oxygen were to bind perpendicular (orthogonal) to the plane of the porphyrin? E. What happens to the structure of the porphyrin when oxygen dissociates from hemoglobin?