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- 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?One molecule of 2,3-bisphosphoglycerate (BPG) binds to one molecule of haemoglobin (Hb) in a central cavity of the haemoglobin molecule. Is the interaction between BPG and Hb stronger or weaker than it would be if BPG were bound to the surface of the protein instead? Explain your answer.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.
- hi 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.Pathological changes in the liver and brain were found in a 27-year-old patient. A diagnosis was Wilson's disease.a) What protein deficiency is observed? What class of globulin does it belong to?b) What is the biological role of this proteinc) The exchange of which trace element is disturbed under these conditions and how will its content in blood plasma and urine change?Sickle-cell hemoglobin (HbS) differs from normal human adult hemoglobin (HbA) by a single mutational change, Glu6 S Val, which causes the HbS molecules to aggregate under proper conditions. Under certain conditions, the HbS filaments that form at body temperature disaggregate when the temperature is lowered to 0°C. Explain.
- 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!)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?Hemoglobin (Hb) is a blood protein that is responsible for transporting oxygen. It can exist in the protonated form as HbH*. The binding of oxygen can be represented by the simplified equation HbH+ + 02 > ABO2 + Ht A. Excessive vomiting may lead to metabolic alkalosis, in which [H2O*] in blood decreases. How does this condition affect the ability of Hb to transport O2? B.Diabetes mellitus may lead to metabolic acidosis, in which [HgO*] in blood How does this condition affect the ability of Hb to transport O?
- Given: Factor VIIa is a man-made protein analog to Factor VII, which is involved in coagulation. (Answer a, b, and c)a. Identify both a competitive and non-competitive inhibitor for Factor VIIa b. Draw a graph showing how both of these molecules will change the Velocity/[S] graph, and explain why this is the case. c. What would a graph look like if both inhibitors were added?A crocodile, which can remain underwater without breathing for up to 1 hour drowns its air-breathing prey, then dines at its leisure. An adaptation that aids the crocodile in doing so is that it can utilize virtually 100% of the O2 in its blood whereas humans, for example, can only extract about 65% of the O2 in their blood. Crocodile Hb does not bind BPG. However, crocodile deoxyHb preferentially binds HCO3-. How does this help the crocodile obtain its dinner? Please help explain why/if this is the answer, thank you! As CO2 concentrations increase so will the concentration of HCO3-. The HCO3- preferentially binds to the crocodile's deoxyhemoglobin, which allosterically prompts the hemoglobin to assume the deoxy conformation and thus release its O2.Apohemoglobin (apoHb) is a dimeric globular protein with two vacant heme‐binding. The preparationof apoHb is based on partial hemoglobin (Hb) unfolding to facilitate heme extraction into an organic solvent. What is an appropriate method for removing the heme? a. An acidic buffer to protonate the His axial ligand in the presence of ureaas the denaturing agent. b. An acidic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent. c. A basic buffer to deprotonate the His axial ligand in the presence of ureaas the denaturing agent. d. An basic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent.
