9) How many peptide fragments would you expect to generate from reacting the following amino acid sequence with the hydrolytic enzyme trypsin, followed by a reaction with cyanogens bromide? LPETYADFHGWQPLMNCVSDEJHGAQJIYTL
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A:
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- The figure shows interaction of various amino acids (Phe, Arg, and Asn) present in Hb with 2,3-DPG. The side chains of these amino acids and 2,3-DPG interactions are circled in red. HO Но Phe HN Asn H2N NH Arg You identify a mutant version of the globin chain where the Arg in circle 2 is replaced with aspartic acid in a patient. Would the Hb protein in this patient be able to transport oxygen even in the presence of 2,3-DPG? ASPARTIC ACID (asp) No, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind oxygen and not 2,3 DPGThere are almost 500 naturally occurring variants of hemoglobin. Most are the result of a single amino acid substitution in a globin polypeptide chain. Some variants produce clinical illness, though not all variants have deleterious effects. A brief sample follows.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
- Relative to the position of hemoglobin A on your gel, where would you expect to find a mutant hemoglobin in which the b-chain glutamic acid residue was replaced by lysine? Sample Wall Number: 1. Normal Hemoglobin- Homoglobin AA 2. Sickle Trait Hemoglobin- Hemoglobin AS 3. Sickle Cell Hemoglobin- Hemoglobin SS 4. The unkniwn hemoglobin sample (showing the mutant sickle cell anemia trait)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 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…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?
- Approximate nH for each protein from its Hill plot. Which proteins exhibits a greater degree of positive cooperativity, normal hemoglobin or the mutant hemoglobin?How does hydroxyurea therapy alleviate the symptoms of sickle cell anemia? (Select all that apply.) HbS dilutes HbF and thus somewhat relieves the symptoms of the disease. HbF dilutes HbS and thus somewhat relieves the symptoms of the disease. HbF, because of its amino acid sequence, does not sickle and clog capillaries. O Hydroxyurea enhances the production of sickle-cell hemoglobin (HbS) in the bone marrow. Hydroxyurea enhances the production of fetal hemoglobin (HbF) in the bone marrow. O HbS, because of its amino acid sequence, does not sickle and clog capillaries.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.
- 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 (A)oxygen affinity, (B)the Bohr effect, and (C)the Hillcoefficient? Explain your answers.{1q}. 1. Why is cyanmethemoglobin method preferred than other methods? 2. In what circumstances is the copper sulfate method used? 3. Discuss the synthesis and breakdown of hemoglobin.?The FIGURE 1 below shows the Bohr shift occurs in fetal haemoglobin (P and Q) and for maternal haemoglobin (R and S). 100 90 80 P pH 7.6, Q pH 7.4 70 60 R pH 7.6 -S pH 7.4 50 40 30 20 10 20 40 60 80 100 120 Po,(mm Hg) FIGURE 1 a) Define Bohr shift. State the effect of Bohr shift on the oxygen dissociation curve. b) Compare the oxygen dissociation curve for fetal and maternal haemoglobin. Explain. c) What happens to the oxygen dissociation curves when the pH is lowered? Explain. d) Give TWO reasons why an expectant mother is advised to give up the smoking. e) Sketch the curve for fetal myoglobin at pH 7.6. Label the curve as X. Percent O2 saturation of hemoglobin