enzymes and proteins

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  • protein structure and enzymes
    • structure
      • primary
        • sequece of amino acids joined by a peptide bond
          • determines 2+3 structure at parts of the chain
      • secondary
        • h bonding forming simple structures eg alpha helix or beta sheet
      • tertiary
        • 3D folding, interactions between groups  - depends where R groups are to where bonds form
          • specific structure forms function
          • -disulphide bridges          -ionic bond.   -hydrogen bonds              -hydrophobic interactions
      • quaternary
        • more than one polypeptide chains
    • enzymes
      • have specific tertiary structure meaning it has a specific active site which is complemtarty to its substrate
      • forms enzyme-substrate complex - stresses bonds
      • induced fit modle
        • enzyme changes shape slightly to better fit substrate which stresses bonds
      • conditions
        • ph -can stress hydrogen bonds ect changing tertary structure - decreasing E-S complexes
          • ror- increases until optimum
        • temp- increased tem= increased Ke therefore more succeful collisons - more e-s complexes
          • moles vibrates and breaks bonds
        • substrate concerntration- more avalible to bind and form e-s complexs
          • sub = more than enzyme - rate = constant
      • inhibitors
        • bind to enzyems and prevent formation of enzyme-substrate complexes
        • competive - binds to active site
        • non-competive binds to enzyme and changes tertary struture of (A~S) no longer complemtary


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