write the mechanism for the reaction of CO2 and the amino terminal of the alpha-1 chain of hemoglobin
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- A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?How does the difference between the-chain and the -chain of hemoglobin explain the differences inoxygen binding between Hb A and Hb F?Describe the secondary and quaternary structure of the red blood cell protein hemoglobin. Which chain of the protein carries mutations causing sickle cell anemia?
- 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?. What would you predict to be the relative rate of synonymous and nonsynonymous substitutions in a globinpseudogene?What is the name of themolecule that transportsoxygen in red blood cells?
- What physiological effect would you predict from a mutation that replacedwith serine the cysteine in the constant part of the immunoglobulin lightchain that is involved in disulfide-bond formation with the heavy chain?(as shown)CYP2E1 has a much higher Km for ethanol than ADH (11 mM versus 0.05 mM,respectively). When greater portions of ethanol are ingested (0.08% or 17 mM), which part of the statement would be true?Describe the secondary structure of the blood protein hemoglobin.
- 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?how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...Fetal hemoglobin binds to BPG to a lesser extent than does HbA because His 143 in the BPG binding pocket in β-globin has been replaced with a serine residue in γ-globin. As a result of the loss of two positive charges (one for each of two γ-globins), the binding pocket binds BPG less avidly. What are the consequences of this phenomenon for mother and fetus?