HIV Protease Mechanism and Inhibitors
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Questions and Answers

What is the primary role of the HIV protease enzyme?

  • To synthesize RNA
  • To replicate DNA
  • To transport molecules across membranes
  • To cleave peptide bonds (correct)
  • What structural feature is critical for the binding of HIV protease inhibitors?

  • A main chain with a hydroxyl group near an aliphatic side chain
  • A cyclic structure that mimics the enzyme's substrate
  • A double bond adjacent to the hydroxyl group
  • A hydroxyl group positioned next to a benzyl group side chain (correct)
  • Which mechanism does the HIV protease utilize to catalyze the cleavage of peptide bonds?

  • Acid-base catalysis with a metal ion
  • Covalent catalysis with an amino acid residue
  • General base catalysis involving water (correct)
  • General base catalysis involving a hydroxyl ion
  • What do the aromatic groups in the HIV protease inhibitors primarily target?

    <p>The aromatic binding pocket of the protease</p> Signup and view all the answers

    How do HIV protease inhibitors mimic the tetrahedral intermediate during catalysis?

    <p>By having a hydroxyl group and a benzyl group</p> Signup and view all the answers

    Which type of amino acids have non-polar, aliphatic R groups?

    <p>Non-polar, aliphatic R groups</p> Signup and view all the answers

    What is a key factor determining the function of a protein?

    <p>The amino acid sequence</p> Signup and view all the answers

    Which protein structure is characterized by the association of multiple polypeptide chains?

    <p>Quaternary structure</p> Signup and view all the answers

    Which of the following proteins is primarily involved in oxygen transport in muscle?

    <p>Myoglobin</p> Signup and view all the answers

    What structural role do proteins play related to bone and connective tissue?

    <p>Provide the matrix for structural integrity</p> Signup and view all the answers

    Study Notes

    HIV Protease

    • Cleaves peptide bonds between phenylalanine (Phe) and proline (Pro) residues in polyproteins
    • Active site contains a pocket for binding aromatic groups

    Mechanism of Action

    • Uses general base catalysis involving water to attack the carbonyl carbon
    • Forms a tetrahedral intermediate
    • Releases the amino acid leaving group while protonating it

    HIV Protease Inhibitors

    • Structurally diverse but share a common core structure: a main chain with a hydroxyl group next to a benzyl group side chain
    • Target the aromatic binding pocket with the benzyl group
    • Designed based on the transition-state analog
    • The adjacent hydroxyl group mimics the negatively charged oxygen atom of the tetrahedral intermediate
    • The remaining parts of the inhibitors fit into specific crevices on the enzyme surface to enhance binding

    Protein Structure

    • Proteins are made up of 20 different amino acids, each with a unique side chain ("R group") that gives it specific properties.
    • Amino acids are zwitterions, meaning they have both a positive and negative charge at physiological pH.
    • The amino acid sequence of a protein is called its primary structure.
    • The three-dimensional structure of a protein is determined by its primary structure and is critical for its function.
    • Secondary structure refers to local folding patterns within the protein, such as alpha-helices and beta-sheets.
    • Tertiary structure describes the overall 3D shape of a single protein chain.
    • Quaternary structure describes the arrangement of multiple protein subunits in a complex.
    • The peptide bond forms between the carboxyl group of one amino acid and the amino group of another, resulting in a planar peptide group.
    • Sickle-cell anemia is a disease caused by a single amino acid mutation in the beta-globin subunit of hemoglobin.

    Protein Function

    • Proteins perform a wide range of functions in the body, including structural support, catalysis, transport, metabolic control, and contraction.
    • Enzyme proteins catalyze metabolic reactions.
    • DNA-binding proteins regulate gene expression.
    • Hemoglobin and myoglobin transport oxygen.
    • Immunoglobulins and interferon protect against infection.
    • Fibrin helps to stop bleeding.

    Denaturation and Folding

    • Denaturation is the process of unfolding a protein, often caused by heat, pH changes, or chemicals.
    • Protein folding is the process by which a protein takes on its correct 3D structure.

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    Description

    This quiz explores the mechanisms of action of HIV protease, including its active site interactions and catalytic process. Additionally, it examines the structural characteristics of HIV protease inhibitors and their design principles. Test your knowledge on the critical aspects of HIV treatment and enzyme inhibition.

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