1. Which expression below shows hemoglobin bound to a protona. HbH+b. HbO₂H+c. HbBPGd. None of the above2. Does hemoglobin, from you answer choice in question number 1,exist in the high affinity state or the low affinity state? What ishemoglobin's heterotropic ligand, based upon your answer choice inquestion number 1?3. What type of the four catalysis reactions referenced in class isdepicted by Asp52 in the diagram to the right?Mur2AeHAcNHAcÑGluFooAsp82(1)HHCH₂OHGlu00⁰0Asp2HНОOHНGlcNAcCH₂OHHOH HH NACFirst product

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Answered: 1. Which expression below shows…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.
In one type of hemoglobin mutant the amino acid change generates a strong ionic interaction stabilizing the T state conformation, but only under conditions of lower pH, e.g., at pH 7.2 compared to pH 7.6. Explain what effect this mutation would have on the amount of O2 delivered to the tissue. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the R state in tissues.
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
The figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent Interactions
2,3-Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?
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.
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…
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 environments
List 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms
) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.
A variant of hemoglobin (Boston variant; mutation His E7(58)α → Tyr) promotes methemoglobin formation involving the α (alpha) subunits. What is the maximum value of the Hill constant (n) that you could measure for the Boston variant of hemoglobin? log (YO2 / 1 - YO2 ) = log pO2 - logP50 Please break down each step of the Hill equation and explain why the result for n is valid from a logical standpoint.

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