Amino Acid Classification Quiz
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Questions and Answers

What is the main function of starch in plants?

  • Cell wall synthesis
  • Structural support
  • Energy storage (correct)
  • Enzyme activation
  • Which type of bond joins the glucose units in amylose?

  • α-1,4-glycosidic bond (correct)
  • β-1,4-glycosidic bond
  • Peptide bond
  • α-1,6-glycosidic bond
  • What is the approximate ratio of amylose to amylopectin in most starches?

  • 75:25
  • 20:80 (correct)
  • 30:70
  • 50:50
  • Which polysaccharide constitutes almost half of the cell-wall material of wood?

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

    What type of bond joins the glucose units in cellulose?

    <p>β-1,4-glycosidic bond (A)</p> Signup and view all the answers

    In which cells is glycogen primarily stored in the body of a well-nourished adult human?

    <p>Liver and muscle cells (C)</p> Signup and view all the answers

    What gives identity to an amino acid?

    <p>R group (side chain) (D)</p> Signup and view all the answers

    Which type of amino acid has an additional carboxyl group?

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

    What is the configuration of the vast majority of α-amino acids at the α-carbon?

    <p>L-configuration (B)</p> Signup and view all the answers

    Which amino acid is achiral and does not have a stereocenter?

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

    In which form are amino acids properly written, indicating their charges?

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

    Proline is considered a __________ amino acid because it does not follow the formula for a primary amino acid.

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

    What is the function of a cofactor in an enzyme?

    <p>It is a nonprotein inorganic portion of an enzyme that is necessary for catalytic function. (D)</p> Signup and view all the answers

    What is the Apoenzyme part of an enzyme composed of?

    <p>The protein part only (C)</p> Signup and view all the answers

    What happens when enzyme concentration increases according to Loyola’s statement?

    <p>The rate increases linearly (D)</p> Signup and view all the answers

    What occurs when the optimal temperature for an enzyme-catalyzed reaction is exceeded?

    <p>The reaction rate decreases due to enzyme conformational changes (C)</p> Signup and view all the answers

    Which part of the enzyme is responsible for binding with the substrate during a reaction?

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

    What effect does pH have on the rate of an enzyme-catalyzed reaction?

    <p>Leads to denaturation of the enzyme (C)</p> Signup and view all the answers

    What is the typical range of carbon atoms found in fatty acids?

    <p>12-20 (A)</p> Signup and view all the answers

    Which of the following fatty acids is considered rare due to its trans isomer predominance?

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

    Why do unsaturated fatty acids generally have lower melting points compared to saturated fatty acids?

    <p>They contain double bonds that introduce kinks (B)</p> Signup and view all the answers

    What type of compounds are triglycerides and what are they composed of?

    <p>Esters; glycerols and fatty acids (D)</p> Signup and view all the answers

    Why are only even-numbered fatty acids found in triglycerides?

    <p>Due to the acetate units used by the body to build these acids (C)</p> Signup and view all the answers

    Why are triglycerides considered the most common lipid materials?

    <p>As they contain long hydrocarbon chains causing hydrophobic character (C)</p> Signup and view all the answers

    What happens when a strong acid is added to an amino acid zwitterion?

    <p>The strong acid donates a proton to the carboxyl group, turning the zwitterion into a positive ion (A)</p> Signup and view all the answers

    At low pH, what is the protonation status of the amino and carboxyl groups in an amino acid?

    <p>Amino group protonated, carboxyl group deprotonated (C)</p> Signup and view all the answers

    What is the acidic form of an amino acid zwitterion at high pH?

    <p>Neutral ion with deprotonated carboxyl group (C)</p> Signup and view all the answers

    What defines the isoelectric point of an amino acid?

    <p>Equal number of positive and negative charges in the sample (B)</p> Signup and view all the answers

    What happens when a strong base is added to an amino acid zwitterion?

    <p>Proton transferred from NH3+ group to the base, turning zwitterion into a negative ion (D)</p> Signup and view all the answers

    What do low and high pH values correspond to in terms of the protonation status of an amino acid?

    <p>Low pH: Fully protonated; High pH: Fully deprotonated (B)</p> Signup and view all the answers

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