1.Hemoglobin is a complex protein that contains four polypeptide chains. The normal hemoglobin found in adults...
1.Hemoglobin is a complex protein that contains four polypeptide chains. The normal hemoglobin found in adults –called adult hemoglobin –consists of two alpha and two beta polypeptide chains, which are encoded by different loci. Sickle-cell hemoglobin, which causes sickle-cell anemia, arises from a mutation in the beta chain of adult hemoglobin. Adult hemoglobin and sickle-cell hemoglobindiffer in a single amino acid: the sixth amino acid from one end in adult hemoglobin is glutamic acid, whereas sickle-cell hemoglobin has valine at this position. After consulting the genetic code in the figure provided in the previous question, indicate the type and location of the mutation that gave rise to sickle-cell anemia.
Homework Answers
Sickle cell anemia is caused due to a point mutation which changes just one nucleotide in the gene for β-globin. This mutation causes the hemoglobin in red blood cells to distort to a sickle shape when deoxygenated. The sickle-shaped RBCs clog in the capillaries, blocking blood flow. The mutation causing sickle cell anemia is a single nucleotide substitution (A to T) in the codon for amino acid 6 from the N-terminus of the peptide chain. This change converts a glutamic acid codon (GAG) to a valine codon (GUG). This is a missense type of point mutations that changes the meaning of the 6th codon from glutamic acid to valine. The hemoglobin in persons with sickle cell anemia is represented as HbS.
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1.Hemoglobin is a complex protein that contains four polypeptide
chains. The normal hemoglobin found in adults...
Sickle cell anemia is a genetic disease resulting from a single amino acid substitution (glutamate to...
Sickle cell anemia is a genetic disease resulting from a single amino acid substitution (glutamate to valine in the sixth position, or E6V) in the hemoglobin β chain. This mutation causes hemoglobin to polymerize into strands in the deoxygenated state, leading to the erythrocytes forming a sickled shape. Speculate as to why the mutation leads to the polymerization of hemoglobin and why this only happens in the deoxygenated state.
Review Questions BIOL 260: Chapters 8-10, 13, 19 1. Consider a mutation involving the deletion of...
Review Questions BIOL 260: Chapters 8-10, 13, 19 1. Consider a mutation involving the deletion of either 1, 2, or 3 nucleotides in the DNA of a bacterium. Which of these mutations (ie., deletion of 1, 2, or 3 nucleotides) would likely have the LEAST impact on the organism? Why? Include in your answer a comparison with the other two options to justify your reasoning. Think carefully about the impact each mutation would have on the ultimate protein coded for...
Detection of Sickle-Cell Disease by Gel Electrophoresis Firee samples of hemoglobin have been subjected to protein...
Detection of Sickle-Cell Disease by Gel Electrophoresis Firee samples of hemoglobin have been subjected to protein gel electrophoresis. Protein gel electrophoresis different composition. ) is carried out in the same manner as DNA gel electrophoresis (see Fig. 10.8) except the gel hasa 1. Sickle-cell hemoglobin (Hb) migrates more Figure 10.10 Gel slowly toward the positive pole than normal hemoglobin (Hb) because the amino acid valine has no polar R groups, whereas the amino acid +Pole glutamic acid does have a...
Human adult hemoglobin is a tetramer containing two alpha (α) and two beta (β) polypeptide chains....
Human adult hemoglobin is a tetramer containing two alpha (α) and two beta (β) polypeptide chains. The α gene cluster on chromosome 16 and the β gene cluster on chromosome 11 share amino acid similarities such that 61 of the amino acids of the α-globin polypeptide (141 amino acids long) are shared in identical sequence with the β-globin polypeptide (146 amino acids long). How might one explain the existence of two polypeptides with partially shared function and structure on two...
Please answer all.... Thank you! 81)If a polypeptide chain contains 600 amino acids, then the gene...
Please answer all.... Thank you!
81)If a polypeptide chain contains 600 amino acids, then the
gene coding for this polypeptide must contain _____.
600 nucleotides
1200 nucleotides
1800 nucleotides
1800 codons
1800 anticodons
More than one of the above are correct.
82) When we altered gene triplet in the DNA produces a chain-terminating codon in the mRNA, the (1pts) result is called a reverse mutation nonsense mutation missense mutation spontaneous mutation frameshift mutation 83) A single base substitution changes the...
In plain language, describe what the oxygen-hemoglobin dissociation curve shows. Under normal conditions, the curve can...
In plain language, describe what the oxygen-hemoglobin
dissociation curve shows. Under normal conditions, the curve can
shift to the right and left. A right shift can be induced by
increased temperature and lower pH among other things. Describe
what a right shift means in terms of hemoglobin’s relationship to
oxygen. In your answer, be sure you address what is actually
happening at the level of the protein (hemoglobin is a protein).
Discuss what types of molecular interactions that can cause...
Case 8 Hemoglobin, the Oxygen Carrier Focus concept A mutation in the gene for hemoglobin results...
Case 8 Hemoglobin, the Oxygen Carrier Focus concept A mutation in the gene for hemoglobin results in an altered protein responsible for the disease sickle cell anemia. An understanding of the biochemistry of the disease may suggest possible treatments Prerequisite Hemoglobin structure and function concepts Background Normal adult hemoglobin is called Hemoglobin A (Hb A). Ninety-eight percent ofaduk hemoglobin is Hb A and 2% is Hb A. There are other forms of hemoglobin. For example, the deve loping fetus has...
Which of the following statements Explain primary, secondary, tirtially and quaternary structures of protien Questions for...
Which of the following statements Explain primary,
secondary, tirtially and quaternary structures of protien
Questions for G2: 1) Would you expect to find valine and leucine on the outside or the inside of the tertiary structure? Why? pts) 2) State whether the following statement describe primary, secondary, tertiary, or quaternary protein (15 pts) structure A. Adjacent chains of polypeptides are held together by hydrogen bonds between the O of the carbonyl group of one chain and the H of an...
match the conditions and the pathogenic mechanisms Temporary suppression of erythropoiesis following a viral infection (often...
match the conditions and the pathogenic mechanisms
Temporary suppression of erythropoiesis following a viral infection (often a Parvovirus B19 infection in a child) Choose Aplastic anemia resulting from defects in DNA repair mechanisms resulting in increased rates of apoptosis and ineffective erythropoiesis Choose... Sickle Cell Anemia Lack of sufficient iron stores to support erythropoiesis Anemia of Chronic Disease Congenital pure red cell aplasia; likely the result of a failure of red cell progenitors to respond to erythropoietic cytokines Fanconi Anemia...
Please check if my answers are correct Temporary suppression of erythropoiesis following a viral infection (often...
Please check if my answers are correct
Temporary suppression of erythropoiesis following a viral infection (often a Parvovirus B19 infection in a child) Transient Erythroblastopenia of Childhood - Aplastic anemia resulting from defects in DNA repair mechanisms resulting in increased rates of apoptosis and ineffective erythropoiesis Fanconi Anemia Lack of sufficient iron stores to support erythropoiesis Iron Deficiency Anemia Congenital pure red cell aplasia; likely the result of a failure of red cell progenitors to respond to erythropoietic cytokines Diamond-Blackfan...
Review Questions BIOL 260: Chapters 8-10, 13, 19 1. Consider a mutation involving the deletion of either 1, 2, or 3 nucleotides in the DNA of a bacterium. Which of these mutations (ie., deletion of 1, 2, or 3 nucleotides) would likely have the LEAST impact on the organism? Why? Include in your answer a comparison with the other two options to justify your reasoning. Think carefully about the impact each mutation would have on the ultimate protein coded for...
Detection of Sickle-Cell Disease by Gel Electrophoresis Firee samples of hemoglobin have been subjected to protein gel electrophoresis. Protein gel electrophoresis different composition. ) is carried out in the same manner as DNA gel electrophoresis (see Fig. 10.8) except the gel hasa 1. Sickle-cell hemoglobin (Hb) migrates more Figure 10.10 Gel slowly toward the positive pole than normal hemoglobin (Hb) because the amino acid valine has no polar R groups, whereas the amino acid +Pole glutamic acid does have a...
Please answer all.... Thank you!
81)If a polypeptide chain contains 600 amino acids, then the
gene coding for this polypeptide must contain _____.
600 nucleotides
1200 nucleotides
1800 nucleotides
1800 codons
1800 anticodons
More than one of the above are correct.
82) When we altered gene triplet in the DNA produces a chain-terminating codon in the mRNA, the (1pts) result is called a reverse mutation nonsense mutation missense mutation spontaneous mutation frameshift mutation 83) A single base substitution changes the...
In plain language, describe what the oxygen-hemoglobin
dissociation curve shows. Under normal conditions, the curve can
shift to the right and left. A right shift can be induced by
increased temperature and lower pH among other things. Describe
what a right shift means in terms of hemoglobin’s relationship to
oxygen. In your answer, be sure you address what is actually
happening at the level of the protein (hemoglobin is a protein).
Discuss what types of molecular interactions that can cause...
Case 8 Hemoglobin, the Oxygen Carrier Focus concept A mutation in the gene for hemoglobin results in an altered protein responsible for the disease sickle cell anemia. An understanding of the biochemistry of the disease may suggest possible treatments Prerequisite Hemoglobin structure and function concepts Background Normal adult hemoglobin is called Hemoglobin A (Hb A). Ninety-eight percent ofaduk hemoglobin is Hb A and 2% is Hb A. There are other forms of hemoglobin. For example, the deve loping fetus has...
Which of the following statements Explain primary,
secondary, tirtially and quaternary structures of protien
Questions for G2: 1) Would you expect to find valine and leucine on the outside or the inside of the tertiary structure? Why? pts) 2) State whether the following statement describe primary, secondary, tertiary, or quaternary protein (15 pts) structure A. Adjacent chains of polypeptides are held together by hydrogen bonds between the O of the carbonyl group of one chain and the H of an...
match the conditions and the pathogenic mechanisms
Temporary suppression of erythropoiesis following a viral infection (often a Parvovirus B19 infection in a child) Choose Aplastic anemia resulting from defects in DNA repair mechanisms resulting in increased rates of apoptosis and ineffective erythropoiesis Choose... Sickle Cell Anemia Lack of sufficient iron stores to support erythropoiesis Anemia of Chronic Disease Congenital pure red cell aplasia; likely the result of a failure of red cell progenitors to respond to erythropoietic cytokines Fanconi Anemia...
Please check if my answers are correct
Temporary suppression of erythropoiesis following a viral infection (often a Parvovirus B19 infection in a child) Transient Erythroblastopenia of Childhood - Aplastic anemia resulting from defects in DNA repair mechanisms resulting in increased rates of apoptosis and ineffective erythropoiesis Fanconi Anemia Lack of sufficient iron stores to support erythropoiesis Iron Deficiency Anemia Congenital pure red cell aplasia; likely the result of a failure of red cell progenitors to respond to erythropoietic cytokines Diamond-Blackfan...
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