Biochemistry: Peptide Bonds and Metabolism
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Questions and Answers

Which process is directly associated with the formation of a peptide bond?

  • Hydrolysis
  • Oxidation
  • Condensation (correct)
  • Reduction
  • What type of bond is formed between the carboxyl group of one amino acid and the amino group of another during peptide bond formation?

  • Covalent bond (correct)
  • Ionic bond
  • Hydrogen bond
  • Van der Waals interaction
  • What is the primary reason for the partial double-bond character of the peptide bond?

  • Protonation of the nitrogen atom
  • Steric hindrance
  • Resonance between the carbonyl group and the amide nitrogen (correct)
  • Hydrophobic interactions
  • During periods of prolonged fasting, which of the following substances is most likely to contribute to ketoacidosis?

    <p>Acetoacetic acid (C)</p> Signup and view all the answers

    What consequence does the resonance within a peptide bond have on its structure?

    <p>It makes the bond planar and rigid. (A)</p> Signup and view all the answers

    Which metabolic process directly produces sulfuric acid in the body?

    <p>Oxidation of sulfur from amino acids such as cysteine and methionine (C)</p> Signup and view all the answers

    Where does the formation of peptide bonds primarily occur in a cell?

    <p>Ribosomes (B)</p> Signup and view all the answers

    What is the primary function of bicarbonate (HCO₃⁻) in maintaining blood pH?

    <p>To neutralize hydroxide ions (OH⁻), and acids (D)</p> Signup and view all the answers

    Which configuration is typically favored in most peptide bonds and why?

    <p>Trans configuration; it minimizes steric hindrance (C)</p> Signup and view all the answers

    A patient's arterial blood pH is measured to be 7.30. This condition is best described as:

    <p>Acidemia (D)</p> Signup and view all the answers

    In the formation of a dipeptide, how many molecules of water are released?

    <p>One (C)</p> Signup and view all the answers

    Which amino acid is an exception to the rule that favors the trans configuration of peptide bonds?

    <p>Proline (D)</p> Signup and view all the answers

    Which of the following is a primary buffer in blood plasma?

    <p>Bicarbonate buffer system (C)</p> Signup and view all the answers

    Which amino acid possesses a side chain that is negatively charged at physiological pH?

    <p>Glutamate (C)</p> Signup and view all the answers

    Which of the following blood pH values would indicate alkalemia?

    <p>7.50 (A)</p> Signup and view all the answers

    What is the primary characteristic of the histidine side chain that allows it to function in proton transfer reactions?

    <p>Its ability to act as both a hydrogen bond donor and acceptor. (B)</p> Signup and view all the answers

    Which of the following is a positively charged amino acid at physiological pH?

    <p>Lysine (C)</p> Signup and view all the answers

    What is the immediate effect of impaired breathing on the blood's acid-base balance?

    <p>It involves a gain of H+ or loss of HCO3- affecting pCO2 (B)</p> Signup and view all the answers

    Which of these is a metabolic acid formed from the breakdown of proteins that contain phosphorus?

    <p>Phosphoric acid (A)</p> Signup and view all the answers

    What is the significance of the pKa of histidine's imidazole group being close to physiological pH?

    <p>It allows histidine to be either protonated or deprotonated. (D)</p> Signup and view all the answers

    Which of the following describes the concept of chirality in amino acids?

    <p>The inability of a molecule to be superimposed on its mirror image. (C)</p> Signup and view all the answers

    What characteristic of histidine makes its charge state sensitive to its local environment when it is part of a protein?

    <p>The presence of delocalized electrons in its imidazole ring. (D)</p> Signup and view all the answers

    Which of the following is NOT a part of the basic structure of an amino acid?

    <p>A phosphate group. (A)</p> Signup and view all the answers

    In the context of oxygen binding in hemoglobin, how does the protonation state of histidine vary between venous and arterial blood?

    <p>The protonation state varies, influencing hemoglobin's ability to bind or release oxygen. (B)</p> Signup and view all the answers

    Which characteristic of the alpha carbon makes most amino acids chiral?

    <p>It is bonded to four different chemical groups. (D)</p> Signup and view all the answers

    Which form of amino acids are commonly found in naturally occurring proteins?

    <p>L-form (A)</p> Signup and view all the answers

    Why is glycine considered achiral?

    <p>Its R group is a hydrogen atom, making two groups on the alpha carbon identical. (A)</p> Signup and view all the answers

    What is the primary role of essential amino acids in humans?

    <p>Protein synthesis (B)</p> Signup and view all the answers

    Which of the following is NOT an essential amino acid for adults?

    <p>Arginine (C)</p> Signup and view all the answers

    What process are proteinogenic amino acids directly involved in?

    <p>Assembly of proteins on the ribosome (A)</p> Signup and view all the answers

    What is the significance of L-amino acids with regards to protein synthesis in mammals?

    <p>They are the active configuration used. (C)</p> Signup and view all the answers

    If a person has a deficiency in dietary essential amino acids, which biological process would most likely be directly affected?

    <p>Protein creation (A)</p> Signup and view all the answers

    What is the primary reason aspirin, a weak acid, is predominantly absorbed in the intestines despite being in an uncharged form in the stomach?

    <p>The larger surface area of the intestinal wall due to villi and microvilli greatly enhances absorption. (A)</p> Signup and view all the answers

    Aspirin is a weak acid with a pKa of 4. How would the ratio of protonated to unprotonated aspirin molecules change in an environment with a pH of 2.0?

    <p>The ratio of protonated to unprotonated molecules would favour the protonated form. (B)</p> Signup and view all the answers

    Why might the unprotonated form of aspirin become trapped within stomach mucosal cells?

    <p>The mucosal intracellular pH favors the ionized form leading to trapping and crystallization. (C)</p> Signup and view all the answers

    Which of the following statements best describes the relationship between pKa and acid strength?

    <p>A higher pKa indicates a weaker acid, with less ionization at a given pH. (A)</p> Signup and view all the answers

    How is the active form of aspirin produced in the body?

    <p>By the removal of an acetyl group in the stomach via enzymatic action. (B)</p> Signup and view all the answers

    If a drug is a weak base, how does a higher pH environment affect its ability to permeate through cell membranes?

    <p>It enhances permeability by favoring the uncharged form of the drug. (B)</p> Signup and view all the answers

    Why is the stomach considered a poor site for drug absorption despite having an acidic environment that favors the uncharged form of weak acids like aspirin?

    <p>The stomach lining is not well adapted for drug absorption, plus it has slow gastric emptying. (A)</p> Signup and view all the answers

    In the context of drug absorption, what determines the effective concentration of the permeable form of a weakly acidic drug at its absorption site?

    <p>The relative concentrations of the charged and uncharged drug forms. (C)</p> Signup and view all the answers

    What is a key differentiating factor between polymorphisms and mutations based on their frequency in a population?

    <p>Mutations occur at a frequency of 1% or lower, while polymorphisms are more frequent. (B)</p> Signup and view all the answers

    How do Human Leukocyte Antigen (HLA) protein variations impact the immune system?

    <p>They result in differences in immune responses, for example, in tissue rejection after organ transplants. (B)</p> Signup and view all the answers

    The sickle cell trait, caused by the Glu6Val mutation in the HBB gene, is maintained in malaria-endemic regions primarily because it:

    <p>Provides a survival advantage by conferring resistance to malaria. (A)</p> Signup and view all the answers

    What determines the diverse range of eye colors such as brown, blue, green and hazel?

    <p>Genetic variations in the OCA2 and HERC2 genes. (C)</p> Signup and view all the answers

    Why are mutations often considered harmful in comparison to polymorphisms ?

    <p>Mutations often lead to altered biological function with a higher likelihood of causing disease. (B)</p> Signup and view all the answers

    Variations in eye color do NOT affect:

    <p>An individual’s overall health. (A)</p> Signup and view all the answers

    Polymorphisms are often influenced by several evolutionary pressures. Which of the following is NOT mentioned as one of these?

    <p>Metabolic imbalances. (A)</p> Signup and view all the answers

    How does a Glu6Val amino acid substitution impact the structure of haemoglobin?

    <p>It introduces a significant change in shape although there are similar properties. (D)</p> Signup and view all the answers

    Study Notes

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    Description

    Test your knowledge on the formation and characteristics of peptide bonds, including their role in metabolism and impact on blood pH. This quiz covers essential concepts related to amino acids, dipeptide formation, and related biochemical processes. Evaluate your understanding of these fundamental topics in biochemistry.

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