More Questions from Structure and Properties of Peptides

Biochemistry—Protein Structure and Function Which of the following statements about common protein examples is INCORRECT? (Assume standard textbook definitions for Protein G, fatty-acid binding protein, and hemoglobin.)

Biochemistry Structure and Properties of Peptides Difficulty: Easy
Choose an option
  • A
    Fatty acid binding protein is composed largely of β-sheet (β-barrel) structure.
  • B
    Hemoglobin is a tetramer containing four polypeptide subunits.
  • C
    Protein G contains only α-helix and no β-sheet.
  • D
    Protein G contains both α-helix and β-sheet motifs.
  • E
    All of the above are correct.

Answer

Correct Answer: Protein G contains only α-helix and no β-sheet.

Explanation

Introduction / Context:Proteins exhibit hierarchical structure (primary to quaternary) and recurring secondary motifs like α-helices and β-sheets. This question checks factual knowledge of well-characterized proteins: Protein G, fatty acid binding protein (FABP), and hemoglobin, and asks you to spot the single incorrect statement.

Given Data / Assumptions:

  • Protein G (GB1 domain) is a small fold that includes both α-helix and β-strands.
  • FABPs are classic β-barrel proteins, dominated by β-sheets.
  • Hemoglobin is a tetramer (α2β2 in adult humans).

Concept / Approach:The strategy is to recall hallmark structural facts: (1) GB1 fold is βαβββ, not all-helix; (2) FABP is β-rich; (3) hemoglobin has four subunits and binds oxygen cooperatively via heme groups.

Step-by-Step Solution:

Step 1: Evaluate the FABP claim. FABP forms a β-barrel; thus “largely β-sheet” is correct.Step 2: Evaluate the hemoglobin claim. Adult Hb (HbA) contains four subunits; this is correct.Step 3: Evaluate the Protein G claims. Protein G (GB1) has one α-helix plus several β-strands; therefore the statement “only α-helix” is false, while “contains both α-helix and β-sheet” is true.

Verification / Alternative check:Standard structural biology references and PDB entries for GB1, FABP, and Hb reinforce these canonical facts about their folds and quaternary states.

Why Other Options Are Wrong:

  • FABP largely β-sheet: correct description of a β-barrel fatty-acid binder.
  • Hemoglobin tetramer: correct for adult human hemoglobin.
  • Protein G has both α and β: correct for GB1 fold.
  • “All of the above are correct”: not true because one statement is incorrect.

Common Pitfalls:Confusing “only α-helix” motifs with mixed βα folds; assuming FABP is α-helical because many membrane proteins are helical (FABP is soluble and β-rich).

Final Answer:Protein G contains only α-helix and no β-sheet.

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