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- 1. Hemoglobin F (HbF), known as fetal hemoglobin, is the predominant hemoglobin in the human fetus at 8 weeks of gestation. Because it is gradually replaced by normal HbA, at birth it constitutes approximately 60% of the total hemo- globin, decreasing to less than 1% by 6 months of age. In comparison to normal, adult HbA comprised of two α-chains and two ẞ-chains, HbF is comprised of two a-chains and two y-chains (gamma-chains). Important differences in the amino acid sequence of y-chains compared to ẞ-chains concern the residues that bind 2,3-bisphosphoglycerate (2,3-BPG), as shown in the table on the right. In addition to the sequence differences in the table, the N-terminal amine group of the y- chain is acetylated having an -NH-COCH3 structure com- pared to the -NH3* group of ẞVal-1 in HbA. (a) (' Decide on the basis of the sequence comparison in the table how the interaction of 2,3-BPG with HbF differs from that with HbA. Explain what physiological advantage this difference…8. Name four intracellular mediators that G proteins impact.7. [10'] For a bacteriophage 77, the following data at zero concentration have been obtained: Sedimentation coefficient: $20,w = 453 S. Diffusion coefficient: D₂0. = 6.03×10-8 cm² s¹¹. 20,w Specific volume V20 = 0.639 cm³ g¹ Calculate the molecular mass M of the bacteriophage.
- 2. (a) The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo- globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group of the BPG molecule confer strong, negative electrostatic character to the molecule. B₁-subunit 1. 2. 3. 5. 6. B₁ (b) Mutant Hemoglobin Hb Raleigh Hb Helsinki The mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or in the vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for binding BPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for Hb Raleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substituted by Ala. Hb Rahere Hb Rancho Mirage Hb Little Rock B₂ Hb Ohio Mutation Val (31)Ala Lys(382) Met Lys(382)) Thr His(143)Asp His(3143)Gln a-NHẠ Ala(142)Asp His 2 His 143 BPG His 143 Lys 82 His 2 Rank the affinity of the mutant hemoglobins for…2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?22. Describe the Induced fit of Hemoglobin, Hb (enzyme-like protein) which has quarternary structure and exhibits allosteric activation with cooperativity.
- Name and describe the main fuctional macromolecule found in red blood cells1. In fetal hemoglobin, residue 143 of the beta subunit is a serine rather than the histidine found in adult hemoglobin (see figure on page 9). a) What does this do to the charges in the BPG binding cavity? b) Would you expect this to change the oxygen affinity of fetal hemoglobin, and, if so, in what direction?6. A quantitative amino acid analysis reveals that bovine serum albumin (BSA) contains 0.58% tryptophan (MW=204) by weight. (a) Calculate the minimum molecular weight of BSA (i.e., assume there is only one Trp residue per protein molecule). (b) Gel filtration of BSA gives a molecular weight estimate of 70,000. How many Trp residues are present in a molecule of serum albumin?
- 1. A mixture of proteins with the following properties were purified using cation exchange chromatography. Which of the following peaks correspond to the correct protein?Protein M- pI- 11, size- 60 KdaProtein N- pI- 8, size- 112 KdaProtein O- pI- 6, size- 280 KdaProtein P- pI- 4, size- 36 Kda[N.B: I was trying to upload pictures, but it was interrupting, Peak C is the highest peak, Peak D is lowest, Peak B is higher than D; however lower than C and A, Peak A is lower than C only, higher than B and D] a) Peak A is P b) Peak C in N c) Peak D is P d) Peak B is O e) Peak A is M 2. Which transition state analog is the most effective competitor for serine protease such as Chymotrypsin?a) R-C=O-NH-R’b) R-C=O(CH3)-NH-R’c) R-CH(OH)-CH(NH2)-R’d) R-CH(OH)-NH-R’e) R-CH=NR’ 3. If a 14C fatty acid labelled with C14 is fed to a cow, after 30 minutes of Beta oxidation, where will the C14 be found?a) Acetyl coA b) Propionyl coA c) Glutamine d) Glucose 4. How many carbons will…1. Researchers isolated a monomeric protein from platelets that has 2 binding sites (A and B) for ADP; Site A's Ka is 157 μM, and Site B's Kd is 2.2 μM. 1.1. A) Which binding site has higher affinity for ADP? B) Briefly justify your answer. C) For this higher affinity site, calculate the standard free energy change for ADP binding. Show your work. 1.2. What concentration of ADP is required to get site A filled in 20% of the proteins? 1.3. Based on this information, sketch a graph of the fraction of site B filled as a function of [ADP].Which of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.