Protein levels

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  • Created by: Jasmin
  • Created on: 19-10-13 18:16
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  • Proteins - levels of structure
    • Primary: sequence of AAs in the chain/protein, joined by peptide bonds
      • Determines eventual shape
        • Change in any of the AA will disturb bonding in 2, 3 levels
      • Change in AA leads to change in shape of protein and may stop it from carrying out its function
    • Secondary: the coiling or folding parts of a protein molecule due to formation of H bonds formed as protein is synthesised
      • Coil into alpha helix or fold into beta pleated sheet
      • H bonds form between the AAs in the chain
    • Tertiary: overall 3D of shape. Result of interaction between parts of protein molecule such as H, disulphide, ionic bonding, interactions
      • Coiled or folded chains coil or fold further
      • Disulphide bonds
        • Strong, not easily broken
        • Less frequent than H bonds, more bonds form due to interactions between R groups of polypeptide chain
        • Form between R groups containing sulphur bonds
      • Ionic bonds
        • Form between R groups with charges +ve and -ve
        • Easily broken by changes in pH
      • H bonds
        • Weak, but numerous
        • Lots of them together make a molecule hold its shape
          • But individually easily broken down
      • Hydrophobic: inside don't like water, Hydrophilic: outside, attracted to water
    • Quaternary: Protein consists of more than one polypeptide chain. Haemoglobin/Insulin
      • How chains are put together
      • Haemoglobin- 4 polypeptide chains bonded together. Determines final structure
  • Quaternary: Protein consists of more than one polypeptide chain. Haemoglobin/Insulin
    • How chains are put together
    • Haemoglobin- 4 polypeptide chains bonded together. Determines final structure

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