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?
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- In an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?A) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?
- In sickle-cell disease, as a result of a single amino acid change, the mutant hemoglobin tetramers associate with each other and assemble into large fibers. Based on this information alone, what does the sickle-cell hemoglobin exhibit? A) only altered primary structure B) only altered tertiary structure C) only altered quaternary structure D) altered primary structure and altered quaternary structure; the secondary and tertiary structures may or may not be alteredOne 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). (Please provide clear and sufficient explanation for the question, thank you!)A) describe in molecular detail how protonation of the histidine side-chain results in hemoglobin's lower affinity for oxygen. b) what value do you expect for the pKa of the histidine side-chain ionizable group?
- The molecular formula for glucose is C6H12O6. What would be the molecular formula for a polymer made by linking ten glucose molecules together by dehydration reactions? Group of answer choices A. C60H120O60 B. C60H102O51 C. C60H100O50 D. C60H111O51 Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)In sickle-cell disease, as a result of a single amino acid change, the mutant hemoglobin tetramers associate with each other and assemble into large fibers.…A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.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.
- Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity?Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity (Please provide clear and sufficient explanation for each part, thank you!)Highly active muscles generate lactic acid by respiration so fast that the blood bassing through the muscle actually experiences a drop in pH from 7.4 to 7.2. Under these conditions, hemoglobin releases about 10% more O2 than it does at pH 7.4. Explain.