... their side chains. Basic amino acids have amine functional groups in their side chains. If the state of ionisation of amino acids in a protein is altered then the ionic bonds that help to determine the 3-D shape of the protein can be altered. This can lead an enzyme becoming inactive. This is known as denaturing. When an enzyme is denatured the tertiary structure is altered, this affects the structure of the active site. If the active site's structure is changed then, following the 'lock & key' theory, it no longer compliments the structure of the substrate and it can no longer bind. No ES complexes are formed and the reaction is not catalysed. At each pH the amount of oxygen evolved increased at a fairly constant rate, producing a reasonably steady gradient, this suggests the rate of catalysation altered very little during the five minutes. In Conclusion: The amount of ...

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