how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...
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- The α and β subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, in the subunits of hemoglobin, certain residues that are hydrophilic in myoglobin are hydrophobic. Why might this be the case?The subunits of hemoglobin and myoglobin share structural similarities. Some residues are hydrophilic in hemoglobin but are hydrophilic in myoglobin. Give an explanation as to why this may be the case.What qualitative effect would you expect each of the following to have on the Pgp of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chains
- What are two features D-Glucosaminate-6-phosphate Ammonia-lyase structure that make either it different OR similar to haemoglobin?What is inositol trisphosphate (IP3)?Cows that graze on spoiled sweet clover, which contains dicoumarol, die from hemorrhagic disease. The cause of death is defective prothrombin. However, the amino acid composition of the defective prothrombin is identical to that of normal prothrombin. What is the mechanism of action of dicoumarol? Why are the amino acid compositions of the defective and normal prothrombin the same?
- How does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein structure (the sum of all the folded protein chains)?Amino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.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.
- How does sickle cell hemoglobin differ from normal hemoglobin at the fourth level of protein structure (the sum of all the folded protein chains)?A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.How does the difference between the-chain and the -chain of hemoglobin explain the differences inoxygen binding between Hb A and Hb F?