What qualitative effect would you expect each of the following to have on the Ps0 of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chains
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- What qualitative effect would you expect each of the following to have on the Pgp of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chains2. (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…Upon binding of oxygen to a hemoglobin subunit, the iron in the center of the heme group moves approximately 0.05 nanometers in distance. Explain, to the extent that we discussed in class, how this SUPER small change in structure contributes to the cooperativity of hemoglobin
- The α and β subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, in the subunits of hemoglobin, certain residues that are hydrophilic in myoglobin are hydrophobic. Why might this be the case?You have an aqueous solution of hemoglobin (pl = 6.8) at pH 6.5, and currently the proteins are soluble. If you had 1 M HCl and 1M NaOH at your disposal, what could you do to precipitate the albumin out of solution? O add NaOH to the solution add HCl to the solution add NaOH to the solution, then add equal volume of HCl to the solution O add HCl to the solution, then add equal volume of NaOH to the solution An error has been detected in your answer. Check for typos, miscalculations etc. before submitting your answer. Submit Answer Try Another Version 1 item attempt remainingYou have an aqueous solution of hemoglobin (pl = 6.8) at pH 5.2, and currently the proteins are soluble. If you had 1M HCl and 1M NaOH at your disposal, what could you do to precipitate the albumin out of solution? add NaOH to the solution O add HCl to the solution O add NaOH to the solution, then add equal volume of HCl to the solution O add HCl to the solution, then add equal volume of NaOH to the solution
- 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.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.How does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein structure (the sum of all the folded protein chains)?
- Calculate the pH of a blood plasma sample with a total CO2 concentration of 26.9 mM and bicarbonate concentration of 25.6 mM. Recall from page 67 that the relevant pK2 of carbonic acid is 6.1(b) Why does solution pH affect separation of proteins via electrophoresis? (c) With reference to a labelled diagram, what is the principle of separation via capillary zone electrophoresis (CZE)?Amino acid analysis of the peptide angiotensin II shows the presence of eight different aminoacids in equimolar amounts: Arg, Asp, His, Ile, Phe, Pro, Tyr and Val. Partial hydrolysis ofangiostensin II with dilute HCl yields the following fragmentsa.) Asp –Arg- Val –Tyr b.) Ile –his –Proc.) Pro –Phe d.) Val – tyr – Ile –His a.)What is the sequence of angiostensin II and what Fragment would result if angiotensin II were cleaved with trypsin? Withchymotrypsin?
