Proteins: Rossmann Fold and Cofactors Quiz
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Questions and Answers

What is the main function of the Rossmann Fold motif in proteins?

  • Aid in the formation of transmembrane structures
  • Create specific microenvironments for protein folding
  • Promote the binding of cofactors (correct)
  • Organize amino acids into parallel beta sheets
  • Which type of interactions play a crucial role in organizing the hydrophobic core of globular proteins?

  • Hydrogen bonding
  • Hydrophobic interactions (correct)
  • Disulfide bonds
  • Ionic interactions
  • What is the primary purpose of organizing amino acid chemistries into specific microenvironments in a globular protein?

  • Maintain protein flexibility
  • Facilitate enzymatic reactions (correct)
  • Prevent protein denaturation
  • Enhance protein solubility
  • In protein structures, which feature combines parallel beta sheets with alpha helices?

    <p>Rossmann Fold motif</p> Signup and view all the answers

    What term describes a protein feature that contains both hydrophilic and hydrophobic regions?

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

    How does the Rossmann Fold motif relate to the binding of cofactors in proteins?

    <p>It positions helices and turns to bind with cofactors.</p> Signup and view all the answers

    Which type of protein structure is tightly packed and compact, as opposed to fibrous proteins like collagen?

    <p>Alpha helix</p> Signup and view all the answers

    What type of interaction between helices is essential for interhelix association to occur in protein structures?

    <p>Van der Waals interactions</p> Signup and view all the answers

    Which motif is frequently encountered in globular proteins and consists of the sequence aa bb bbbb?

    <p>Greek Key motif</p> Signup and view all the answers

    What type of interactions are utilized at the helix-helix interface to decrease free energy (DG°) in protein folding?

    <p>Van der Waals interactions</p> Signup and view all the answers

    In an amphipathic structure of a protein, which part of the structure interacts favorably with water?

    <p>Polar region</p> Signup and view all the answers

    What feature permits different angles of helices to be adopted in globular protein folding, leading to diverse functions?

    <p>Linker length between helices</p> Signup and view all the answers

    Why are disulfide bonds important in protein stability?

    <p>They create intrachain covalent linkages that increase protein stability</p> Signup and view all the answers

    Which of the following is NOT a reason why disulfide bonds are not present in every protein?

    <p>Disulfides can form too many hydrophobic interactions</p> Signup and view all the answers

    What property of proteins is used to compare their stability by quantifying the melting temperature (Tm)?

    <p>Degree of native vs unfolded conformation</p> Signup and view all the answers

    In what type of proteins are disulfide bonds mostly found?

    <p>Secreted proteins</p> Signup and view all the answers

    Which structure in proteins is primarily stabilized by hydrophobic interactions?

    <p>Amphipathic structures</p> Signup and view all the answers

    What is the significance of breaking only one of the disulfide bonds in a protein like bovine pancreatic trypsin inhibitor?

    <p>It decreases protein stability significantly</p> Signup and view all the answers

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