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Protein Structure and Folding Quiz
48 Questions
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Protein Structure and Folding Quiz

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Questions and Answers

What stabilizes protein structures?

  • Hydrophobic effect only
  • Ionic interactions only
  • Covalent interactions only
  • Noncovalent interactions and forces (correct)

    • What determines the tertiary structure of a protein?

  • Quaternary structure
  • Amino acid sequence (correct)
  • Secondary structure
  • Peptide bonds

    • What impacts the formation of regular secondary structures in proteins?

  • Tertiary structure
  • Amino acid composition (correct)
  • Peptide bonds
  • Quaternary structure

    • What describes the interactions between components of a multisubunit assembly?

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

    What plays an important role in the initial folding of polypeptides?

    <p>Local secondary structures</p> Signup and view all the answers

    Which protein is required for the folding of proteins that do not fold spontaneously?

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

    What is the molecular basis for many human genetic disorders related to protein folding?

    <p>Defects in protein folding</p> Signup and view all the answers

    What protein is associated with extracellular amyloid deposition in Alzheimer's disease?

    <p>Amyloid-β peptide</p> Signup and view all the answers

    Which protein is involved in the intracellular aggregation in Huntington disease?

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

    What is the protein associated with misfolded brain protein in prion diseases?

    <p>Prion protein (PRP)</p> Signup and view all the answers

    What is the study of three-dimensional structures of biomolecules, including proteins, nucleic acids, lipid membranes, and oligosaccharides?

    <p>Structural biology</p> Signup and view all the answers

    What catalyzes the interchange, or shuffling, of disulfide bonds in proteins?

    <p>Protein disulfide isomerase (PDI)</p> Signup and view all the answers

    What do structural biologists use various methods to solve?

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

    What largely stabilizes a protein's conformation?

    <p>Weak interactions</p> Signup and view all the answers

    What contributes hydrogen bonds and ion pairs to protein folding?

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

    What limits the range of conformations a protein can assume?

    <p>Peptide bond rigidity</p> Signup and view all the answers

    What favors protein folding by decreasing solvation layer entropy?

    <p>Hydrophobic effect</p> Signup and view all the answers

    What is a common protein secondary structure, with every backbone N−H group hydrogen bonding to the backbone C=O group of the amino acid that is four residues earlier in the protein sequence?

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

    What promotes protein folding by combining weak interactions?

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

    What involves pathways regulating protein folding, unfolding, and degradation?

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

    What causes many human diseases?

    <p>Protein misfolding and defects in proteostasis</p> Signup and view all the answers

    What do native proteins exist in?

    <p>Functional, folded conformations</p> Signup and view all the answers

    What is included in protein secondary structure?

    <p>α helix, β conformation, β turn, and random coils</p> Signup and view all the answers

    What do proteins assume without breaking covalent bonds?

    <p>Countless conformations</p> Signup and view all the answers

    What confers significant stability to the helical backbone?

    <p>Intrahelical hydrogen bonds between specific amino acid residues</p> Signup and view all the answers

    Why do Proline and Glycine occur infrequently in an α helix?

    <p>Proline and Glycine have destabilizing and flexible nature, respectively</p> Signup and view all the answers

    What does circular dichroism spectroscopy differentiate between in proteins?

    <p>Different secondary structures</p> Signup and view all the answers

    What does the tertiary structure of a protein refer to?

    <p>The overall three-dimensional arrangement of atoms in a protein</p> Signup and view all the answers

    What type of proteins give strength and flexibility to structures?

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

    What influences the stability of the α helix?

    <p>Amino acid sequence and interactions between R chains</p> Signup and view all the answers

    What organizes polypeptide chains into sheets in the β conformation?

    <p>β turns</p> Signup and view all the answers

    Which type of β sheets are more frequently found in natural proteins?

    <p>Antiparallel β sheets</p> Signup and view all the answers

    What does the quaternary structure of a protein involve?

    <p>The arrangement of multiple polypeptide chains in three-dimensional complexes</p> Signup and view all the answers

    How can common secondary structures in proteins be visualized and assessed?

    <p>Using Ramachandran plots</p> Signup and view all the answers

    What do globular proteins have a more compact and diverse tertiary structure adapted for?

    <p>Various biological functions</p> Signup and view all the answers

    What influences the stability of the α helix near the end of the segment?

    <p>Small electric dipoles aligning through hydrogen bonds</p> Signup and view all the answers

    What does the PDB ID represent?

    <p>Experimental 3D structures with atomic coordinates and accuracy information</p> Signup and view all the answers

    What do folding patterns of proteins involve?

    <p>Motifs, recognizable folding patterns, and domains</p> Signup and view all the answers

    What is the basis for protein structural classification in the PDB and SCOP2 database?

    <p>Protein motifs</p> Signup and view all the answers

    What represents the relationships among segments of secondary structure in a protein?

    <p>Topology diagrams</p> Signup and view all the answers

    What do protein families and superfamilies involve?

    <p>Proteins with significant similarity in primary and tertiary structure</p> Signup and view all the answers

    What does denaturation cause?

    <p>Loss of three-dimensional structure and function</p> Signup and view all the answers

    What is the process by which denatured globular proteins regain their native structure and biological activity?

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

    What facilitates functional promiscuity and interaction with multiple binding partners?

    <p>Intrinsically disordered segments</p> Signup and view all the answers

    What is the continual maintenance of the active set of cellular proteins required under given conditions known as?

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

    What range do quaternary structures involve?

    <p>From simple dimers to large complexes</p> Signup and view all the answers

    What do amino acid sequence determine?

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

    What are complex motifs built from?

    <p>Simple motifs</p> Signup and view all the answers

    Study Notes

    Protein Structure and Folding: Key Concepts

    • PDB ID is assigned to experimentally determined 3D structures with data files containing atomic coordinates, structure determination, and accuracy information
    • Folding patterns of proteins involve motifs, recognizable folding patterns, and domains, independently stable parts of a polypeptide chain
    • Protein-folding rules such as burial of hydrophobic R groups, α helices, and β sheets in different layers, and stable folding patterns
    • Complex motifs are built from simple motifs, and some proteins or segments are intrinsically disordered lacking definable structure
    • Intrinsically disordered segments can assume different structures, facilitating functional promiscuity and interaction with multiple binding partners
    • Protein motifs form the basis for protein structural classification in the PDB and SCOP2 database, with a limited number of folding patterns
    • Topology diagrams represent the relationships among segments of secondary structure in a protein
    • Protein families and superfamilies involve proteins with significant similarity in primary and tertiary structure, with strong evolutionary relationships
    • Quaternary structures range from simple dimers to large complexes, involving the assembly of multiple peptide subunits
    • Proteostasis involves the continual maintenance of the active set of cellular proteins required under given conditions, with protein denaturation and folding pathways involved
    • Denaturation causes loss of three-dimensional structure and function, occurring through heat, pH extremes, and other factors, leading to protein precipitation
    • Amino acid sequence determines tertiary structure, and renaturation is the process by which denatured globular proteins regain their native structure and biological activity

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    Related Documents

    Week 3-3D structure of protein.pdf

    Description

    Test your knowledge of protein structure and folding with this quiz covering key concepts such as PDB IDs, protein motifs, intrinsically disordered segments, quaternary structures, proteostasis, denaturation, and renaturation. Explore the fundamental principles governing the 3D organization and function of proteins.

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