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 ofthe BPG molecule confer strong, negative electrostatic character to the molecule.B₁-subunit1.2.3.5.6.B₁(b)Mutant HemoglobinHb RaleighHb HelsinkiThe mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or inthe vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for bindingBPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for HbRaleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substitutedby Ala.Hb RahereHb Rancho MirageHb Little RockB₂Hb OhioMutationVal (31)AlaLys(382) MetLys(382)) ThrHis(143)AspHis(3143)Glna-NHẠAla(142)AspHis 2His 143BPGHis 143Lys 82His 2Rank the affinity of the mutant hemoglobins for binding BPG.a-NH,*B2-subunitExplanation of effect of mutation on BPGbinding

To comprehend the BPG binding site within hemoglobin, it's important to note that it resides within…

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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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10. In an abnormal hemoglobin variant known as Hemoglobin-Kariya, the lysine residues at position 40 in the ß-chains are replaced by glutamic acid residues. a) What effect would you expect this change to have on the quaternary structure and oxygen binding properties of hemoglobin? b) Draw a diagram to illustrate the difference in the oxygen binding curves that would be obtained with normal hemoglobin and Hemoglobin-Kariya.
Two proteins are discovered, and both are shown to have a potential in treating fatty liver disease. The structural differences of the proteins require them to be delivered using spherical nanoparticles made of different polymers. The scientists are trying to decide which protein will be more efficient to use in applications where a faster drug release is more favorable. Protein 1 is loaded into spherical nanoparticles made of polymer 1 which has R=100 nm at a concentration of 50 nM. Protein 2 is loaded into spherical nanoparticles made of polymer 2 which has R=250 nm, at a concentration of 50 nM. The partition coefficient of polymer 1 is 0.01 and is known to be half of partition coefficient of polymer 2. The diffusion coefficient of protein 1 in polymer 1 is 2x10-6 cm2/s, and diffusion coefficient of protein 2 in polymer 2 is 3.4x10-6 cm2/s. Determine which treatment will be selected for treatment of fatty liver disease.
3a) An 68 kg patient is to be given a 2.0 mg/kg body weight IV bolus dose of a newly developed antibiotic drug every 6 hours. Assume the half-life of the drug and its volume of distribution in the patient are 3.2 hours and 0.26 L/kg respectively. (a) Calculate the peak and trough plasma concentrations for the antibiotic after, one dose, two doses, four doses, and at steady state.
Azathioprine is an immunosuppressant drug used in kidney transplants. In vivo, azathioprine is metabolized to the hypoxanthine analog 6- mercaptopurine, which is then converted into 6-mercaptopurine ribose monophosphate, the active form of the drug. 6- Mercaptopurine ribose monophosphate also inhibits de novo purine synthesis, reducing uric acid levels in the blood and urine. However, when administered to Lesch – Nyhan patients, there was no effect on uric acid levels. Explain why this is the case.
9. If 32p-labeled inorganic phosphate were introduced to erythrocytes undergoing glycolysis which of the following molecules would you NOT expect to detect 32p in? ** Multiple answers: Multiple answers are accepted for this question a. Fructose 1-6 bisphosphate b. 3-Phosphoglyceraldehyde c. Dihydroxyacetone phosphate d. 2-Phosphoglycerate e. 1-3 bisphosphoglycerate f. Phosphoenolpyruvate g. 3-Phosphoglycerate h. Pyruvate i. Glucose 6-Phosphate
Give the effect of the following changes in the protein structure of hemoglobin Replacement of analanine located at the middle of helix B with proline
a) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?
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 the Hill coefficient
3. The image below depicts 2,3-bisphosphoglycerate depicted in dark gray, and ß subunits are depicted in light gray. (BPG) bound to hemoglobin. The a subunits are BPG (a) Briefly explain how BPG regulates oxygen transport by hemoglobin and describe the critical chemical properties of BPG and its binding pocket.
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].
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

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