Proteins - AP Biology

  1. What is the role of myosin?
    Motor protein involved in muscle contraction. Converts chemical energy to mechanical force for movement.
  2. Which amino acid is most commonly found in collagen?
    Glycine. Smallest amino acid allows tight turns in collagen helix.
  3. What is the function of rhodopsin?
    Photoreceptor protein in the retina. Light-sensitive protein that initiates vision in rod cells.
  4. Identify the protein responsible for oxygen storage in muscles.
    Myoglobin. Single-chain protein that stores oxygen in muscle tissue.
  5. Which bond is formed between the carboxyl and amino group of two amino acids?
    Peptide bond. Dehydration reaction creates covalent linkage in protein backbone.
  6. Identify a protein involved in immune response.
    Antibodies. Immunoglobulins that provide specific defense against pathogens.
  7. What is the role of elastin?
    Provides elasticity to tissues. Allows tissues to stretch and return to original shape.
  8. Identify the technique used to determine protein structure.
    X-ray crystallography. Uses X-rays to reveal atomic-level protein structure details.
  9. Which structure level involves alpha helices and beta sheets?
    Secondary structure. Formed by hydrogen bonds between backbone atoms in polypeptide.
  10. What is the effect of pH on protein structure?
    Can lead to denaturation. Extreme pH disrupts hydrogen bonds and ionic interactions.
  11. Identify a protein involved in cell signaling.
    Receptors. Membrane proteins that detect and respond to chemical signals.
  12. What is the quaternary structure of proteins?
    Assembly of multiple polypeptide chains. Multiple polypeptides combine to form functional protein complexes.
  13. What is the role of chaperone proteins?
    Assist in protein folding. Prevent misfolding and help proteins achieve proper 3D structure.
  14. Identify one example of a globular protein.
    Hemoglobin. Compact, spherical protein with complex tertiary structure.
  15. What is the role of hemoglobin?
    Transport oxygen in blood. Iron-containing protein binds and carries oxygen molecules.
  16. What type of interaction stabilizes tertiary protein structure?
    Hydrophobic interactions, disulfide bridges. Side chain interactions create and maintain 3D protein shape.
  17. What is the impact of temperature on enzyme activity?
    High temperature can denature enzymes. Extreme heat breaks bonds that maintain enzyme active site.
  18. Which structure is the sequence of amino acids in a polypeptide?
    Primary structure. Foundation level that determines all higher structural levels.
  19. What are enzymes?
    Proteins that act as biological catalysts. Speed up biochemical reactions by lowering activation energy.
  20. What is a protein domain?
    Functional unit within a protein. Independently folded region with specific structure and function.
  21. Which enzyme is involved in DNA replication?
    DNA polymerase. Synthesizes new DNA strands during cell division.
  22. Which amino acid initiates protein synthesis?
    Methionine. Start codon AUG codes for this first amino acid.
  23. Which amino acid has a sulfur atom in its side chain?
    Cysteine. Only amino acid capable of forming disulfide bonds.
  24. What is denaturation in proteins?
    Loss of structure and function. Disruption of non-covalent bonds destroys protein's native shape.
  25. What is the role of insulin?
    Regulates blood glucose levels. Hormone that lowers blood sugar by promoting glucose uptake.
  26. Identify a method to separate proteins based on size.
    Gel electrophoresis. Separates proteins by molecular weight through porous gel matrix.
  27. What determines the primary structure of a protein?
    Amino acid sequence. Linear order of amino acids determines all higher-level structures.
  28. Identify the bond formed between cysteine residues.
    Disulfide bond. Covalent sulfur-sulfur bridge stabilizes protein structure.
  29. What is the function of antibodies?
    Bind to antigens to neutralize them. Y-shaped proteins that recognize and bind specific foreign substances.
  30. Identify one example of a fibrous protein.
    Collagen. Structural protein with elongated, rope-like quaternary structure.
  31. Which protein structure is affected by denaturation?
    Secondary, tertiary, quaternary structures. Higher-order structures unfold while primary structure remains intact.
  32. Name the four levels of protein structure.
    Primary, secondary, tertiary, quaternary. Hierarchical organization from amino acid sequence to complex 3D shape.
  33. Identify the bond that links amino acids in proteins.
    Peptide bond. Covalent bond formed by dehydration synthesis between amino acids.
  34. What is the monomer unit of proteins?
    Amino acids. Basic building blocks that link together to form protein chains.
  35. Identify the protein that acts as a buffer in blood.
    Albumin. Most abundant blood protein that maintains osmotic pressure.
  36. What is the role of ferritin?
    Stores iron in cells. Storage protein that safely sequesters iron for cellular use.
  37. What is the role of catalase?
    Breaks down hydrogen peroxide. Antioxidant enzyme that protects cells from oxidative damage.

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