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Questions and Answers
Which of the following is true about the HBB gene mutation?
Which of the following is true about the HBB gene mutation?
- It is an integral component of coenzyme A, essential for the TCA cycle and fatty acid metabolism.
- It can cause aberrant splicing of pre-mRNA, leading to reduced levels of functional beta-globin protein and anemia. (correct)
- It leads to elevated levels of HbF and detectable HbA1 in a specific form of B-thalassemia.
- It is involved in the production of prostaglandins.
What is the function of telomeres?
What is the function of telomeres?
- They contribute to the stability of the triple helix structure of collagen chains.
- They are essential for the TCA cycle and fatty acid metabolism.
- They are involved in the production of prostaglandins.
- They are specialized structures at chromosome ends, maintained by telomerase to protect DNA from degradation during replication. (correct)
What is the primary composition of collagen chains?
What is the primary composition of collagen chains?
- Tyrosine and tryptophan, crucial for signal transduction.
- Glutamine and asparagine, essential for protein synthesis.
- Proline and glycine, contributing to the stability of the triple helix structure. (correct)
- Adenine and thymine, forming the base pairs of DNA.
What is the role of aspirin and ibuprofen?
What is the role of aspirin and ibuprofen?
What is the role of the anomeric carbon in carbohydrates?
What is the role of the anomeric carbon in carbohydrates?
What is the common theme in DNA binding proteins' structure?
What is the common theme in DNA binding proteins' structure?
Which amino acid side chains can be phosphorylated by protein kinases?
Which amino acid side chains can be phosphorylated by protein kinases?
What is the likely cause of elevated serum amylase and lipase levels in a 48-year-old man with acute abdominal pain?
What is the likely cause of elevated serum amylase and lipase levels in a 48-year-old man with acute abdominal pain?
What type of enzyme kinetics are common for multimeric enzymes, showing cooperative binding of substrates and allosteric modulation?
What type of enzyme kinetics are common for multimeric enzymes, showing cooperative binding of substrates and allosteric modulation?
Which method cannot detect fructose as a reducing sugar?
Which method cannot detect fructose as a reducing sugar?
Which type of amino acids are more likely to be exposed to water in a folded protein structure?
Which type of amino acids are more likely to be exposed to water in a folded protein structure?
What is the likely cause of fetal warfarin syndrome in children of mothers taking warfarin during pregnancy?
What is the likely cause of fetal warfarin syndrome in children of mothers taking warfarin during pregnancy?
What is the primary role of retinal, a form of vitamin A?
What is the primary role of retinal, a form of vitamin A?
Which group is involved in the conversion of B-carotene to retinal in the intestinal mucosa?
Which group is involved in the conversion of B-carotene to retinal in the intestinal mucosa?
Which type of protein modification is phosphorylation?
Which type of protein modification is phosphorylation?
Where do non-polar amino acids usually form a cluster in a helical protein?
Where do non-polar amino acids usually form a cluster in a helical protein?
What type of amino acids are more likely to be found in the interior of a folded protein?
What type of amino acids are more likely to be found in the interior of a folded protein?
What is the prosthetic group of rhodopsin?
What is the prosthetic group of rhodopsin?
What type of bond is formed between two sugar molecules through the reaction between the anomeric carbon of one sugar and the hydroxyl group of another sugar?
What type of bond is formed between two sugar molecules through the reaction between the anomeric carbon of one sugar and the hydroxyl group of another sugar?
What is the common structural motif found in many DNA binding proteins, involved in the recognition and binding of specific DNA sequences?
What is the common structural motif found in many DNA binding proteins, involved in the recognition and binding of specific DNA sequences?
What type of bonds do DNA binding proteins form with DNA?
What type of bonds do DNA binding proteins form with DNA?
What enzyme is responsible for removing the phosphate group from phosphorylated amino acid residues, thus reversing the effects of kinases?
What enzyme is responsible for removing the phosphate group from phosphorylated amino acid residues, thus reversing the effects of kinases?
What process do synthetases catalyze by joining two substrates using ATP?
What process do synthetases catalyze by joining two substrates using ATP?
What is the major attractive force between DNA and proteins, allowing the formation of specific types of DNA-protein complexes during the cell cycle?
What is the major attractive force between DNA and proteins, allowing the formation of specific types of DNA-protein complexes during the cell cycle?
What transports retinol to the liver after processing by the intestinal mucosa?
What transports retinol to the liver after processing by the intestinal mucosa?
What enzyme hydrolyzes glycosidic bonds, which are covalent bonds that link a sugar molecule to another molecule?
What enzyme hydrolyzes glycosidic bonds, which are covalent bonds that link a sugar molecule to another molecule?
What is responsible for cleaving B-carotene in the intestinal mucosa, yielding retinal?
What is responsible for cleaving B-carotene in the intestinal mucosa, yielding retinal?
What can phosphorylation of specific amino acid residues in proteins do to the function of enzymes, membrane transporters, and other proteins?
What can phosphorylation of specific amino acid residues in proteins do to the function of enzymes, membrane transporters, and other proteins?
How many possible configurations (R and S) do chiral carbon atoms in sugars have?
How many possible configurations (R and S) do chiral carbon atoms in sugars have?
What is a common mechanism for regulating cellular signaling pathways and controlling various cellular processes such as metabolism, growth, and differentiation?
What is a common mechanism for regulating cellular signaling pathways and controlling various cellular processes such as metabolism, growth, and differentiation?
Which amino acids can be ionizable in water due to certain side chains or carboxyl groups?
Which amino acids can be ionizable in water due to certain side chains or carboxyl groups?
What is the primary protein structure of hemoglobin and myoglobin?
What is the primary protein structure of hemoglobin and myoglobin?
Which coenzyme is required for the action of pyruvate carboxylase?
Which coenzyme is required for the action of pyruvate carboxylase?
What gene mutations lead to Wilson's disease?
What gene mutations lead to Wilson's disease?
Which of the following is a characteristic of the genetic code?
Which of the following is a characteristic of the genetic code?
Why are enzymes effective catalysts?
Why are enzymes effective catalysts?
What is the primary function of alpha-1-antitrypsin?
What is the primary function of alpha-1-antitrypsin?
Do enzymes catalyze reactions that would not occur at all?
Do enzymes catalyze reactions that would not occur at all?
How do enzymes affect the equilibrium point of reactions?
How do enzymes affect the equilibrium point of reactions?
What change do enzymes bring to the rate of both forward and reverse reactions?
What change do enzymes bring to the rate of both forward and reverse reactions?
What does alpha-1-antitrypsin compromise in the alpha1-globulin fraction of normal serum?
What does alpha-1-antitrypsin compromise in the alpha1-globulin fraction of normal serum?
Is alpha-1-antitrypsin involved in the formation of elastin cross-links?
Is alpha-1-antitrypsin involved in the formation of elastin cross-links?
Which of the following amino acids is considered hydrophobic at physiological pH of 7.4?
Which of the following amino acids is considered hydrophobic at physiological pH of 7.4?
In B-thalassemia, patients with significantly reduced levels of B-globin transcripts and elevated levels of HbF exhibit no detectable HbA1 due to:
In B-thalassemia, patients with significantly reduced levels of B-globin transcripts and elevated levels of HbF exhibit no detectable HbA1 due to:
Which of the following amino acid side chains may be considered as hydrophobic at physiological pH of 7.4?
Which of the following amino acid side chains may be considered as hydrophobic at physiological pH of 7.4?
In B-thalassemia, patients with significantly reduced levels of B-globin transcripts and elevated levels of HbF exhibit no detectable HbA1 due to:
In B-thalassemia, patients with significantly reduced levels of B-globin transcripts and elevated levels of HbF exhibit no detectable HbA1 due to:
What is a common mechanism for regulating cellular signaling pathways and controlling various cellular processes such as metabolism, growth, and differentiation?
What is a common mechanism for regulating cellular signaling pathways and controlling various cellular processes such as metabolism, growth, and differentiation?
What is the major attractive force between DNA and proteins, allowing the formation of specific types of DNA-protein complexes during the cell cycle?
What is the major attractive force between DNA and proteins, allowing the formation of specific types of DNA-protein complexes during the cell cycle?
Which of the following amino acid side chains may be considered as hydrophobic at physiological pH of 7.4?
Which of the following amino acid side chains may be considered as hydrophobic at physiological pH of 7.4?
In B-thalassemia, patients with significantly reduced levels of B-globin transcripts and elevated levels of HbF and no detectable HbA1 exhibit these observations due to:
In B-thalassemia, patients with significantly reduced levels of B-globin transcripts and elevated levels of HbF and no detectable HbA1 exhibit these observations due to:
Which of the following forms of amino acid side chains can form hydrogen bonds with water molecules?
Which of the following forms of amino acid side chains can form hydrogen bonds with water molecules?
In hemoglobin, which amino acid is responsible for the nonpolar side chain that is hydrophobic?
In hemoglobin, which amino acid is responsible for the nonpolar side chain that is hydrophobic?
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Study Notes
Biochemistry and Genetics Summary
- Polar amino acids with certain side chains or carboxyl groups can be ionizable in water.
- Hemoglobin and myoglobin primarily consist of alpha helices, a common secondary protein structure.
- Pyruvate carboxylase deficiency requires biotin as a coenzyme for its action.
- Wilson's disease is caused by mutations in the ATP7B gene and leads to copper accumulation in the body.
- The genetic code is degenerate, unambiguous, nonoverlapping, without punctuation, and universal.
- Enzymes are effective catalysts because they decrease the free energy of activation of reactants.
- Alpha-1-antitrypsin inhibits neutrophil elastase and is involved in elastin biosynthesis.
- Enzymes do not catalyze reactions that would not occur at all or shift the equilibrium of reactions toward more complete conversion to product.
- Enzymes increase the rate of both the forward and reverse reactions equally, without affecting the equilibrium point of the reaction.
- Enzymes do not affect the standard free energy change (∆G 0) of reactions, only reducing the activation energy of the reaction.
- Alpha-1-antitrypsin compromises more than 90% of the alpha1-globulin fraction of normal serum and is mainly produced in the liver.
- Alpha-1-antitrypsin inhibits N- or C-terminal procollagen peptidases and is not involved in the formation of elastin cross-links.
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