Justify all answers (show all work).1. Minor changes in primary structure can have pronounced effects on biological function. Tetramerichemoglobin, a₂³₂, dissociates into pairs of dimers aß to different extents depending on the protein primarystructure. The standard Gibb energies of dissociation of normal adult hemoglobin A and of several mutantshave been determined and are listed in the table below.Substitution in mutantHemoglobinA, normalRichmondKansasGeorgia102B; Asn → Thr102B; Asn → Thr95x; Pro → LeuAG® of dissociation (kcal/mole Hb)8.26.0655.13.6(a) Write an equilibrium expression for the dissociation of hemoglobin tetramer into dimers.(b) For normal hemoglobin and its three mutants (variations) calculate the equilibrium constant for theirdissociation from a tetramer into dimers.(c) How do the equilibrium constants for the dissociation of the hemoglobin mutants compare to that ofnormal hemoglobin?

Hemoglobin is a tertameric protein made up of 4 subunits namely α2β2. The αβ form a dimer and 2 such…

Answered: 1. Minor changes in primary structure…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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Normal Hgb is referred to as HbA and contains 4 subunits, 2 α-globin chains and 2 β-globin chains, arranged as two dimers of αβ. In Sickle Cell Disease, both β-globin chains are altered in the dimers (αβS/αβS). Q3: Which level of structure does the αβ/αβ and αβS/αβS in HbA and HbS describe?
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
3 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.
A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.
Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)Which of the following statements about hemoglobin is most consistent with the information in the passage? Group of answer choices A. a tertiary protein with two polypeptides B. a quaternary protein with two polypeptides C. a tertiary protein with four polypeptides D. a quaternary protein with four polypeptides When nucleotides polymerize to form a nucleic acid, ________. Group of answer choices A. a…
Use the information on the proteins given to solve the questions: A. Draw a UV-Vis spectrum of each protein (A, B, C, and D) from 240 – 480 nm if they were all present at 20 µM. B. How can you create a two-step purification procedure that could be used to purify protein A from the other proteins. In addition, include a chromotagram as well.
The hemoglobin in the fetus (HbF) is a structural variant of the hemoglobin in the mother (HbA). HbA is a tetrameric protein complex consisting of two α-globin and two β-globin subunits. HbF is made up of two αglobin and two γ-globin subunits, where the γ-globins are similar to the β-globins but γglobins have lower affinity for 2,3- bisphosphoglycerate or BPG. Studies of oxygen transport in pregnant mammals show that the oxygen-saturation curves between the red blood cells of the fetus and the mother are markedly different. 1. The shape of hemoglobin binding curves is: hyperbolic or sigmoidal 2. a) Based on the binding curves, determine the dissociation constant (Kd) for each hemoglobin complex. (Show correct units.) Kd of HbF + BPG: ________________ Kd of HbA + BPG: _____________________ b) Which has a higher affinity for oxygen? HbF+BPG HbA+BPG 3. a) How many BPG molecule(s) is/are expected to bind one hemoglobin complex? 1 2 3 4 b) BPG binding preferentially stabilizes which state…
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?
hi there you have said Microcytic anemia could be caused due to both iron deficiency anemia and thalassemia. could you expalin in detail why and how. With the a of diagram Along with mechanims.
"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?
A) describe in molecular detail how protonation of the histidine side-chain results in hemoglobin's lower affinity for oxygen. b) what value do you expect for the pKa of the histidine side-chain ionizable group?

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