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Tertiary Structure of Protein quiz #1

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  • What is the main difference between secondary and tertiary protein structure in terms of stabilization?
    Secondary structure is stabilized by interactions between the peptide backbone, while tertiary structure is stabilized primarily by interactions between the R groups (side chains) of amino acids.
  • List and briefly describe the five main types of R group interactions that stabilize the tertiary structure of proteins.
    The five main types are: (1) Ionic bonds (salt bridges) between ionizable R groups; (2) Hydrophobic effect, where non-polar R groups cluster together; (3) Hydrogen bonds between polar R groups; (4) Van der Waals interactions between all atoms; (5) Disulfide bridges, which are covalent bonds between cysteine residues.
  • How can amino acid R groups that are far apart in the primary sequence interact in the tertiary structure of a protein?
    Due to the folding of the polypeptide chain in tertiary structure, R groups that are distant in the primary sequence can be brought into close proximity, allowing them to interact and contribute to the protein's three-dimensional shape.
  • What is the main difference between secondary and tertiary protein structure in terms of stabilization?
    Secondary structure is stabilized by interactions between the peptide backbone, while tertiary structure is stabilized primarily by interactions between the R groups (side chains) of amino acids.
  • List and briefly describe the five main types of R group interactions that stabilize the tertiary structure of proteins.
    The five main types are: (1) Ionic bonds (salt bridges) between ionizable R groups; (2) Hydrophobic effect, where non-polar R groups cluster together; (3) Hydrogen bonds between polar R groups; (4) Van der Waals interactions between all atoms; (5) Disulfide bridges, which are covalent bonds between cysteine residues.
  • How can amino acid R groups that are far apart in the primary sequence interact in the tertiary structure of a protein?
    Due to the folding of the polypeptide chain in tertiary structure, R groups that are distant in the primary sequence can be brought into close proximity, allowing them to interact and contribute to the protein's three-dimensional shape.
  • What type of bond is formed between two cysteine residues in a protein's tertiary structure?
    A disulfide bridge, which is a covalent bond, is formed between the sulfur atoms of two cysteine residues.
  • Which type of R group interaction is responsible for the clustering of non-polar amino acids in the interior of a protein?
    The hydrophobic effect causes non-polar R groups to cluster together, helping to stabilize the protein's tertiary structure.
  • What is another name for ionic bonds in the context of protein tertiary structure, and which amino acids typically participate in them?
    Ionic bonds are also called salt bridges, and they typically form between ionizable R groups such as those of lysine and aspartic acid.
  • Why are van der Waals interactions important for tertiary protein structure even though they are weak?
    Van der Waals interactions occur between all atoms in the protein and, collectively, provide a significant stabilizing effect on the tertiary structure.
  • What is the tertiary structure of a protein?
    The tertiary structure of a protein is its overall three-dimensional folded shape, stabilized primarily by interactions between the R groups (side chains) of amino acids, including non-covalent interactions such as ionic bonds, hydrophobic effects, hydrogen bonds, van der Waals interactions, and covalent disulfide bridges.
  • Which types of interactions stabilize the tertiary structure of a protein?
    The tertiary structure of a protein is stabilized by R group interactions, including non-covalent interactions (ionic bonds or salt bridges, hydrophobic effect, hydrogen bonds, van der Waals interactions) and covalent disulfide bridges between cysteine residues.
  • What amino acid forms disulfide bonds in proteins?
    Cysteine is the amino acid that forms disulfide bonds, creating covalent disulfide bridges that help stabilize the tertiary structure of proteins.
  • How can amino acid R groups that are far apart in the primary sequence interact in the tertiary structure of a protein?
    Due to the folding of the polypeptide chain in the tertiary structure, amino acid R groups that are far apart in the primary sequence can be brought into close proximity, allowing them to interact and contribute to the protein's overall three-dimensional shape.