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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 environmentsConsider 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?A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?
- 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.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 oxygenhi there you have said Microcytic anemia could be caused due to both iron deficiency anemia and thalassemia. could you expalin in detail why and how. With the a of diagram Along with mechanims.
- Match the subfamilies of HSPGS withe their examples v syndecans and CD44V3 A. GPI-linked proteoglycans v glypicans B. Membrane-spanning proteoglycans v perlecan and collagen XVII C. Secreted ECM proteoglycans v agrin -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.30. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environments
- 1.1 ;) The diagram on the right compares the O2 binding prop- 1.0 erties or normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(B68)His. In the dia- gram Y = fraction of heme groups with bound O2, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Hb Great Lakes %3D 0.8 Hb A 0.6 Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O2 binding (Ko2) for Y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. 0.4 You need draw only the central, linear portion of the Hill plot. 0.2 F State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 0 10 20 30 40 50 60 pO2 (torr)how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...The action of this enzyme found in Beano alpha-galactosidase can also according to many sources be used to remove ____________ from the red blood cells of the B blood group and convert them to the O blood group. Since the _________ molecules (composed of many monomers) are connnected to protein on the membrane and also the cell membrane of the red blood cell itself; therefore these molecules help create cell identity and recognition, and when the are connected to proteins they are known as _________ , but if they are connected to the cell membrane itself they are known as ____________. This is a good question for reviewing the structures on the cell membrane as well. The only difference between the B-blood type and the O-blood type is ________. The following is a diagram of the differences of these molecules that determine blood type. List of answers: disaccharid, proteins ,dehydration synthesis ,nucleotide ,amino acids ,nucleic acids ,lactose ,fructose ,sucrose ,hydrolysis…