5. Which of the following is true about myoglobin and/or hemoglobin? O (a) The iron in Hb is in the ferric (Fe³+) state (b) Hb is a homotetramer (c) Both myoglobin and hemoglobin contain the same fold of eight a helices O (d) Mb is commonly found in the circulatory system.
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- The primary structure of mammalian hemoglobin, an a202 tetramer, is approximately. O 2% 18% Ο 50% Ο 78% 0 986 identical to myoglobin2. (a) The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo- globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group of the BPG molecule confer strong, negative electrostatic character to the molecule. B₁-subunit 1. 2. 3. 5. 6. B₁ (b) Mutant Hemoglobin Hb Raleigh Hb Helsinki The mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or in the vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for binding BPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for Hb Raleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substituted by Ala. Hb Rahere Hb Rancho Mirage Hb Little Rock B₂ Hb Ohio Mutation Val (31)Ala Lys(382) Met Lys(382)) Thr His(143)Asp His(3143)Gln a-NHẠ Ala(142)Asp His 2 His 143 BPG His 143 Lys 82 His 2 Rank the affinity of the mutant hemoglobins for…3 Myoglobin binds oxygen much more efficiently than hemoglobin. In both cases, the binding of oxygen is accompanied by changes to the geometry of iron coordination. Select the relevant values from the table below and relate them to the lower oxygen affinity of hemoglobin. A discussion of the changes to the protein structure is not required. lon Coordination type Radius / pm Fe(lI) 4-coordinate, tetrahedral 77 Fe(lII) 4-coordinate, tetrahedral 63 Fe(ll) 4-coordinate, square-planar 78 Fe(II) 6-coordinate, octahedral 75 Fe(lI) 6-coordinate, octahedral, high spin 92.0 Fe(lII) 6-coordinate, octahedral 69 Fe(lII) 6-coordinate, octahedral, high spin 78.5 Fe(IV) 6-coordinate, octahedral 72.5 Fe(ll) 8-coordinate 106 Fe(II) 8-coordinate 92
- One 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!)I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role. I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only bind to oxygen, and not release oxygenThe primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.
- 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 environments26. Describe the structure of hemoglobin. 1+ Hemoglobin Location of Hb # of protein chains in 1 molecule of Hb Name of protein in Hb? I # of heme groups in 1 molecule of Hb # of iron atoms in 1 molecule of Hb # of O₂ molecules 1 molecule of HB can transport #of O₂ molecules 6 molecules of Hb can transport Color of blood when O₂ bound to Hb Color of blood when no O₂ bound to Hb Part of Hb that binds to 0₂ Part of Hb that binds to CO₂ Part of Hb that binds to H* ions Which type of Hb (adult or fetal) has a greater affinity (attraction to O2)? What hemoglobin A1C levels measure Description Four protein chains Four heme groups Four iron atoms Four oxygen molecules Bright red Dark red Iron atom 4 iron atoms Fetal HB What % of the patients Hemoglobin is coated with Sugar (glycated)
- 1. What is hemoglobinopathy? What is sickle-cell anemia? Explain the concept relating to protein structure. 2. How does the oxygen-carrying functions of myoglobin differ from that of hemoglobin?One 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).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.