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AP Biology — Unit 1 — Macromolecules & Protein Structure — Drill 1

Drill 1 ·

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About This Drill

AP Biology — Unit 1 — Macromolecules & Protein Structure — Drill 1 is a practice drill. It contains 5 original questions created by Brian Stewart, a Barron's test prep author with over 20 years of tutoring experience.

Practice analyzing protein structure levels and the relationship between amino acid sequence and protein function with this AP Biology drill.

Passage

Biological macromolecules are large molecules assembled from smaller repeating subunits called monomers. The four major classes of macromolecules -- carbohydrates, lipids, proteins, and nucleic acids -- differ in their monomers, bonds, and biological functions. Proteins are the most functionally diverse class, serving as enzymes, structural components, transporters, and signaling molecules. Proteins are polymers of amino acids linked by peptide bonds formed through dehydration synthesis. Each amino acid has a central (alpha) carbon bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable R group (side chain) that determines the amino acid's chemical properties. The sequence of amino acids -- the primary structure -- determines how a protein folds into its final three-dimensional shape. Protein folding proceeds through hierarchical levels of structure. Secondary structure involves local folding patterns -- alpha-helices and beta-pleated sheets -- stabilized by hydrogen bonds between backbone atoms. Tertiary structure is the overall three-dimensional shape of a single polypeptide, stabilized by interactions among R groups including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. Quaternary structure applies to proteins with more than one polypeptide subunit. A researcher studies four proteins and records selected properties in the table below. Protein Subunits Secondary Structure Tertiary Stabilizing Interactions Function W 1 Alpha-helices Hydrophobic interactions Membrane transport X 4 Beta-pleated sheets Ionic bonds, disulfide bridges Structural support Y 1 Alpha-helices + Beta-pleated sheets Hydrogen bonds, hydrophobic inter. Enzyme Z 2 Beta-pleated sheets Disulfide bridges Hormone signaling

Questions in This Drill

  1. Based on the table, which of the following proteins has quaternary structure?
  2. Protein W functions as a membrane transport protein. Based on its predominant secondary structure and key stabilizing interactions, which of the following best explains how Protein W is suited for its function?
  3. A student argues that two proteins with identical primary structures must have identical functions. A researcher responds by describing a scenario in which the same polypeptide sequence folds differently depending on its cellular environment. Which of the following best evaluates the student's claim in light of the researcher's response?
  4. A mutation changes a single amino acid in Protein Y, replacing a hydrophobic R group in the protein's interior with a hydrophilic R group. Which of the following best predicts the consequence of this mutation?
  5. The researcher argues that the diversity of protein functions seen in the table -- transport, structural support, enzyme activity, and hormone signaling -- is ultimately traceable to differences in amino acid sequence. Which of the following best supports this argument?