9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily, metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name and explain the "trick" depicted by images below. In your answer, be certain to explain the effect on hemoglobin structure. 1.0r az Lys 40 *pH 7.6 Y 0.5- `pH 7.4 C terminus pH 7.2 Added proton B, His 146 B, Asp 94 6. 8 10 Fre po, (kPa)

9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily, metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name and explain the "trick" depicted by images below. In your answer, be certain to explain the effect on hemoglobin structure. 1.0r az Lys 40 *pH 7.6 Y 0.5- `pH 7.4 C terminus pH 7.2 Added proton B, His 146 B, Asp 94 6. 8 10 Fre po, (kPa)

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Description: 9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily,metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name andexplain the "trick" depicted by images b

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter6: Basic Clinical Chemistry

Section6.1: Introduction To Clinical Chemistry

Problem 9RQ

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Electrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu - Hb Y: Asp replaced by Leu - Hb Z: Glu replaced by Lys What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.
9. The T conformation of the hemoglobin tetramer is stabilized (in part) by a salt linkage between the side chain of the lysine residue at position 40 in the a-chain of one aß dimer and the C-terminal carboxylate group of the ß-chain of the opposing aß dimer. Draw a diagram of this salt linkage (show complete side chains).
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?
15. An amino acid binding protein in cell membranes has been shown to bind histidine, but only histidine molecules with a net charge of +1. Calculate [His+] in 20 mM histidine solution at pH = 6.4. The pka values for histidine are a-CO2H = 1.82, side chain = 6.00, a-NH3* = 9.17. Show all your work. NH3 HO Histidine (shown in fully protonated form)
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You have discovered a new hemoglobin variant you are calling Hb-21. You have noticed the following from your studies of Hb-21: - The binding constant of Hb-21 is the same at pH 7.1 and 7.4.- The binding constant curves generated by Hb-21 and O2 are sigmoidal.- The Hill coefficient for Hb-21 is 3.-The binding constant for Hb-21 with O2 in the presence of 5mM 2,3-bisphosphglycerate is about 6-times lower instead of the 8-times lower that is observed under these conditions for the wild type enzyme. Use this information to answer questions: Based on this information which of these features of hemoglobin would you conclude are altered in Hb-21 as compared to the wild type hemoglobin? ____ the cooperativity.____ the amount of T versus R state in the tissues. ____ the Bohr effect. What is the major issue for an individual with the Hb-21 variant? Explain exactly what aspect of hemoglobin’s function is altered.
Relatively hydrophobic proteins will require higher amounts of (NH4)2S04 to precipitate.
In 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?
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.
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