Lesson 3.1.4.1.2

3.1.4.1.2 Protein structure: primary to quaternary Quiz: AQA Biology, Unit 1

20 questions

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Lesson 3.1.4.1.2, Protein structure: primary to quaternary: 20 multiple choice questions for the AQA Biology (7402), Unit 1: Biological molecules, written with Revision Ninja.

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The 20 questions

  1. What defines the primary structure of a protein molecule?

    • Globular 3D shape
    • Alpha helix folding
    • Subunit arrangement
    • Amino acid sequence
  2. Which bonds maintain the secondary structure of a protein?

    • Ionic bonds
    • Peptide bonds
    • Disulfide bridges
    • Hydrogen bonds
  3. What level of protein structure involves multiple polypeptide chains joined together?

    • Quaternary structure
    • Primary structure
    • Tertiary structure
    • Secondary structure
  4. How many polypeptide chains does normal adult haemoglobin contain?

    • 1
    • 4
    • 8
    • 2
  5. Which covalent bond stabilises the tertiary structure of a protein?

    • Peptide bond
    • Hydrogen bond
    • Ionic bond
    • Disulfide bridge
  6. Which bond type helps maintain the tertiary structure of a protein?

    • Phosphodiester bond
    • Ester bond
    • Ionic bond
    • Glycosidic bond
  7. A beta-pleated sheet is an example of which level of protein structure?

    • Tertiary structure
    • Primary structure
    • Secondary structure
    • Quaternary structure
  8. Which protein structure level determines how a polypeptide chain folds into its final shape?

    • Quaternary structure
    • Secondary structure
    • Primary structure
    • Prosthetic group
  9. In sickle cell anaemia, substitution of a surface amino acid causes haemoglobin molecules to do what?

    • Denature completely
    • Dissolve completely
    • Hydrolyse rapidly
    • Form long fibres
  10. Breaking disulfide bridges in a protein directly affects which structural level?

    • Secondary structure
    • Tertiary structure
    • Peptide sequence
    • Primary structure
  11. Which level of protein structure remains intact when a protein is denatured by heat?

    • Primary structure
    • Tertiary structure
    • Quaternary structure
    • Secondary structure
  12. Which structural level determines the specific three-dimensional shape of an enzyme active site?

    • Primary structure
    • Quaternary structure
    • Tertiary structure
    • Secondary structure
  13. A protein has three identical polypeptide chains, each with 100 amino acids. How many peptide bonds are present in total?

    • 300
    • 297
    • 303
    • 294
  14. Which property is characteristic of a fibrous protein such as collagen?

    • Spherical shape
    • High tensile strength
    • Metabolic activity
    • High solubility
  15. Which level of protein structure is altered when a protein loses its specific 3D shape?

    • Secondary sequence
    • Peptide structure
    • Primary structure
    • Tertiary structure
  16. Which factor directly dictates how a polypeptide chain folds into its tertiary structure?

    • Substrate concentration
    • Cellular pH
    • Amino acid sequence
    • Peptide bond length
  17. Changes in pH disrupt protein shape primarily by breaking which type of bond?

    • Disulfide bridges
    • Ionic bonds
    • Ester bonds
    • Peptide bonds
  18. What term describes how binding oxygen to one haemoglobin subunit increases affinity in others?

    • End-product inhibition
    • Cooperative binding
    • Competitive inhibition
    • Allosteric degradation
  19. Which quaternary structure gives collagen its high tensile strength?

    • Alpha helix
    • Triple helix
    • Beta-pleated sheet
    • Single coiled strand
  20. Which feature defines the quaternary structure of a protein?

    • Single polypeptide chain
    • Local alpha-helices
    • Amino acid sequence
    • Multiple polypeptide chains

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