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Proteins (4 structure levels (Primary (sequence of amino acids) -Peptide…

- - - - Primary structure -wide rage of amino acids
      - Secondary structure - each polypeptide chain has 8 alpha helices connected by short beta-pleated sheet segments
      - Tertiary structure - contains 'haem' prosthetic group making a conjugated protein. Haemoglobin also contains no disulphide bridges
      - Quaternary structure- contains 4 subunits, 2 beta and two alpha. Each subunit contains a haem prosthetic group
  - - - Primary structure - narrow range of amino acids. Triple sequence (glycine, proline, x) leading to long and unfolded proteins.
      - Secondary & tertiary structure - due to predominance of glycine forms a narrow left-handed helix
      - Quaternary structure - 3 subunits that wind round each other in a right-handed helix and are held by hydrogen bonds. Disulphide cross links hold molecules together forming strong fibres
    - - Primary structure - alternate hydrophobic and lysine-rich areas
      - Secondary & tertiary structure- forms soluble tropoelastin molecules
      - Quaternary structure - the tropoelastin molecules aggregate and form large stable elastin through hydrophobic interactions. This is stabilised through covalent bonds between lysine molecules. This gives it flexibility.