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1 The denaturation of three different proteins (P, Q and R) at different temperatures were investigated. The more denatured a protein is, the less stable the molecule becomes. The following graph shows the results of this investigation.

  • A) Protein R would be less stable and had a lower rate of denaturation above 70°C compared to protein Q, while protein P was fully denatured by 80°C
  • B) Protein R would be more stable and had a lower rate of denaturation above 70°C compared to protein Q, while protein P was the least heat tolerant of all the proteins
  • C) Protein Q would be more stable and had a lower rate of denaturation below 70°C compared to protein R, while protein P was fully denatured by 80°C
  • D) Protein Q would be less stable and had a higher rate of denaturation below 70°C compared to protein R, while protein P was the least heat tolerant of all the proteins
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4 Researchers produced a particular type of reactive molecule, known as a radical, that can interact with a protein’s amino acids at a molecular level. Under certain conditions, the radical molecules selectively react to break carbon-carbon bonds within an amino acid, meaning that protein editing can be achieved. Which of the following best predicts the location of where the radicle interacts?

  • A) Radicles interact with the peptide bond of an amino acid
  • B) Radicles interact with the R-group of an amino acid
  • C) Radicles interact with the amino group of an amino acid
  • D) Radicles interact with the peptide bond of a di-peptide
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5 Proteins play a key role in many biological functions. Insulin is a protein hormone that regulates blood sugar levels. Insulin is composed of chains of amino acids, which are linked together through specic covalent bonds during its synthesis in the pancreas. Which of the following represents the type of bonds that connect the monomers in insulin?

  • A) Monomers in insulin are connected via a peptide bond between the carboxylic groups of two amino acids.
  • B) Monomers in insulin are connected via a peptide bond between the carboxylic group of one amino acid and the amino group of a neighboring amino acid.
  • C) Monomers in insulin are connected via a peptide bond between the amino group of two amino acids.
  • D) Monomers in insulin are connected via a peptide bond between the R group of one amino acid and the amino group of a neighboring amino acid.
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