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  • 1 Proteins

  • 1.1.1 Structure and terminology- amino acids

  • How is a C-atom with different atoms on every side called?

    Chiral atom
  • What is the difference and occurrence of the 2 stereoisomers?

    L is on the left, occurs in nature. D is on the right and is present after processing, it is non-digestible to humans.
  • What is the difference between the alpha and beta amino-acid?

    Alpha is the C atom next to the functional carbonyl (COOH) group, beta is the C atom next to it. Note: both of them can have a NH3 attached.
  • How can amino acids be classified based on side-chain?

    • Non-polar, non-charged
    • Polar, non-charged
    • Polar, charged
  • How can amino acids be classified based on nutritional value?

    • Essential
    • Conditionally essential
    • Non-essential
  • 1.1.2 Structure and terminology- peptides

  • In what situations does the trans or cis conformation of a peptide take place?

    Trans --> in nature

    Cis --> after processing
  • 1.1.3 Structure and terminology- proteins

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  • Mention 3 system conditions that can change the structure of proteins

    1. Temperature
    2. pH and ionic strength
    3. Solvent
  • Which 3 different types of interactions stabilise the quaternary structure of proteins?

    1. Hydrophobic interactions
    2. Disulfide bonds
    3. Charge
  • What can the presence of a reducing agent do to structural forces used for protein folding and stability?

    It can break the disulphide bonds (S-S).
  • 1.1.4 Structure and terminology- protein classification

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  • Give examples of the classes of proteins based on structure and give their natural solubility

    • Globular (blood, soy) --> high
    • Fibrillar (gelatin, meat) --> low
    • Random coil (caseins) --> high
    • Other (gluten) --> low

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