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Concept explainers
Interpretation:
Effect of hemoglobin when substitution of valine for glutamic acid in primary structure of hemoglobin has to be identified.
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino
Primary structure of protein is a sequence in which the amino acids linked by peptide bond in a protein.
Sickle-cell anemia is a hereditary disease caused by genetic difference that replaces one amino acid (glutamate) with another in each of the two polypeptide chains of the hemoglobin.
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Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Edition; Modified Mastering Chemistry with Pearson eText -- ValuePack ... and Biological Chemistry (4th Edition)
- 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?arrow_forwardArginine has three ionizable groups. The pK of α-COOH is 2.18; α-NH 3 + , 9.09; and the R-group, 13.20. What is the isoelectric point of arginine?arrow_forwardWhich structure represents d-erythrose?arrow_forward
- What are two features D-Glucosaminate-6-phosphate Ammonia-lyase structure that make either it different OR similar to haemoglobin?arrow_forwardA) describe in molecular detail how protonation of the histidine side-chain results in hemoglobin's lower affinity for oxygen. b) what value do you expect for the pKa of the histidine side-chain ionizable group?arrow_forwardHow does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein structure (the sum of all the folded protein chains)?arrow_forward
- 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 chainsarrow_forwardHow many hemoglobin molecules are there in an average red cell? Assume that the molecular weight of the human hemoglobin tetramer is 65 kDa.arrow_forwardHow does sickle cell hemoglobin differ from normal hemoglobin at the fourth level of protein structure (the sum of all the folded protein chains)?arrow_forward
- What is the structure of the peptide P-A-I-G-E at a pH of 7 and 12? What is the isoelectric point?arrow_forwardIn 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?arrow_forwardThe pH at which the Lysine R group is 20% dissociated?arrow_forward
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