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- 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?30. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environments2. (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…
- List 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms8. In a patient with anemia, the presence of Heinz bodics in the RBCS was the result of the hemoglobin subunits aggregation due to the oxidation of -SH groups of Hb cysteine residues with active oxygen forms and the formation of disulfide bonds. What metabolic disorders in the RBC can be the cause of this clinical case? To solve the problem: a) indicate which reactions maintain cysteine residues in a reduced state; b) name the coenzyme involved in this process, write a diagram of the process in which the reduced form of this coenzyme is formed; c) indicate the enzyme which deficiency may lcad to a lack of the reduced cocnzyme and be the cause of the clinical case described above."Hemoglobin can be in either an oxy- or deoxy- state at a given pH. Given the appropriate pKa values, calculate fraction protonated at a given pH" How would I do this?
- 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.. In the experiments of Barrick, et al. ( observed that replacement of histidine by a noncovalently bonded imidazole not only reduced cooperativity but also increased the oxy- gen affinity of the hemoglobin. Suggest an explanation. it was2.(a) The two diagrams on the right compare O2 binding pro- perties of Hb Kariya, a human hemo- globin characterized by the mutation Lys(a40)Glu, with those of HbA as a function of pH ranging from pH 9.0 to pH 6.95. One O2 saturation curve () illustrates the O2 binding proper- ties at pH 7.5 in the presence of 2 mM inositol hexaphosphate (IHP). (IHP is found in avian red blood cells. and binds more tightly than BPG be- cause of the additional negative charges.) log [Y/(1 - Y)] Hb Kariya + IHP (b) The diagram on the right illustrates sche- matically the interaction of the side chain of the aLys40 residue with the C-terminal -COOH group of the B-sub- unit in HbA. In Hb Kariya with a Lys(a40)Glu mutation, which allosteric conformation R or T is destabilized, and which allosteric HbA conformation is illustrated on the right? Explain log (P) Excluding the O2 saturation curve collected in the presence of inositol-hexaphosphate (IHP), indicate with an arrow for both hemoglobins the plot…
- In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to (A)oxygen affinity, (B)the Bohr effect, and (C)the Hillcoefficient? Explain your answers.1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…Please fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to the