Given below is the electrophoretic profile of 2 proteins, a normal hemoglobin, HbA and the fetal hemoglobin, HbF. What information can be obtained from the profile shown? (+) HbF ww wm (-) HbA A. HbF has a slightly different conformation compared with HbA B. HbF and HbA have different primary structures C. HbF has a higher affinity for oxygen than HbA D. HbF has a nonpolar amino acid residue in place of a basic amino acid. E. HbF has an acidic amino acid residue in place of a nonpolar amino acid
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- The steps involved in the T→ R transition in when oxygen binds to hemoglobin are outlined below. Place them in the correct order (1 = first thing to happen), assuming that it is the oxygen-binding that initiates the transition and that the process occurs in discrete steps. The proximal histidine is pulled by the heme iron. The F helix is pulled out of place, breaking a network of salt bridges. The iron is pulled into the plane of the protoporphyrin IX ring. Oxygen binds to the heme. < <Which of the following did Ruth Benesch and her husband Reinhold Benesch accomplish? Select all that apply. determining the function of 2-3-biphosphoglyceric acid determined the exact location BPG binds hemoglobin by X-ray analysis predicted the location BPG binds to hemoglobin demonstrated that the alpha and beta heterodimers of hemoglobin and conformational changes in the protein were essential to the function of the protein and its cooperative bindingPlease 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
- 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.Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobinsCertain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobins.b. Are the mildly thalassemic individuals with Leporehemoglobin homozygotes or heterozygotes for theunusual allele?c. Why might these mildly thalassemic people produce less Lepore hemoglobin than normal adulthemoglobin?
- Fetal hemoglobin binds to BPG to a lesser extent than does HbA because His 143 in the BPG binding pocket in β-globin has been replaced with a serine residue in γ-globin. As a result of the loss of two positive charges (one for each of two γ-globins), the binding pocket binds BPG less avidly. What are the consequences of this phenomenon for mother and fetus?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 DPG2B. 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?
- The figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent InteractionsA 30 - year - old woman was undergoing therapy for b-thalassemia,a recessive trait caused by absence of or reduced synthesis ofthe hemoglobin b chain, a subunit of the oxygen-carrying moleculein red blood cells. In this condition, red blood cells are rapidlydestroyed, freeing a large amount of iron, which is deposited in tissuesand organs. The blood transfusions the patient had received every twoor three weeks since the age of 7 to stave off anemia were furtheraggravating iron buildup. Her major organs were showing damage, andshe was in danger of death from cardiac disease. Her physician suggestedthat she consider undergoing a hematopoietic (bone marrow)stem cell transplant (HSCT). Since these stem cells give rise to redblood cells, such a transplant could potentially restore her health. Whilethis might seem like an easy decision, it is not. Advanced cases havea high risk (almost 30 percent) for transplantation-related death. At thispoint, the woman is faced with a difficult and…A 30 - year - old woman was undergoing therapy for b-thalassemia,a recessive trait caused by absence of or reduced synthesis ofthe hemoglobin b chain, a subunit of the oxygen-carrying moleculein red blood cells. In this condition, red blood cells are rapidlydestroyed, freeing a large amount of iron, which is deposited in tissuesand organs. The blood transfusions the patient had received every twoor three weeks since the age of 7 to stave off anemia were furtheraggravating iron buildup. Her major organs were showing damage, andshe was in danger of death from cardiac disease. Her physician suggestedthat she consider undergoing a hematopoietic (bone marrow)stem cell transplant (HSCT). Since these stem cells give rise to redblood cells, such a transplant could potentially restore her health. Whilethis might seem like an easy decision, it is not. Advanced cases havea high risk (almost 30 percent) for transplantation-related death. At thispoint, the woman is faced with a difficult and…