A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in Not enough information Higher than normal binding affinity to oxygen Lower than normal binding affinity to oxygen Normal binding to oxygen
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- In oxygenated hemoglobin, pKa 5 6.6 forthe histidines at position 146 on the -chain. In deoxygenated hemoglobin, the pKa of these residues is 8.2. How can this piece ofinformation be correlated with the Bohr effect?A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in a) Not enough information b) Normal binding to oxygen c) Higher than normal binding affinity to oxygen d) Lower than normal binding affinity to oxygenA 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?
- A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.(No more than one page). Explain why quaternary structure is necessary for cooperativity and allosteric regulation. Use hemoglobin as an example. Include the various allosteric effectors that influence oxygen binding.The transport of aspirin (pKa = 3.5, structure shown here) from the digestive tract to the circulation occurs by nonmediated absorption into cells lining the stomach (where pH = 0.8) and the small intestine (where pH 6.0). Do you expect absorption to be faster in the stomach or in the small intestine?
- The following sequence of amino acids are part of adult hemoglobin from the N-terminus. Draw the skeletal structure of this peptide. Val-His-Leu-Thr-Pro-Glu-Glu-Lys-Ser-Ala-Val-ThrYou have a mixture of 4 amino acids (Q, W, E, R, T) that you want to separate using ion exchange chromatography. Which of these amino acids would bind most strongly to a DEAE anion exchange column at pH 7? Q W E R TWhat is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed values
- how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...Calculate the concentration of the ligand required to fill 25% of the binding site. X+A ⇌ XA , ka = 1.5 ×10-6 Y+A ⇌ YA , ka = 4.7 × 10-4 (i.e, q = 0.25) for both proteins.The production of arginine is terminated by the presence of excess arginine. State which phenomenon is responsible for this outcome. Explain the phenomenon in brief.