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    I understand that if the pH of an enzyme solution is lowered, the H+ ions interact with the R - groups in the tertiary structure to a point that the enzyme becomes denatured.

    What happens if the pH is raised above the optimum pH?
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    If the pH of a solution is too high (i.e too far above the optimum pH) then there are too many OH- ions which- similarily to the H+ ions in too acidic solutions- then go on to interact with the ionic and hydrogen bonds in the enzymes tertiary structure, causing the bonds to break and the enzymes active site consequently changes and becomes permanently denatured.
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    (Original post by Elishchambers)
    If the pH of a solution is too high (i.e too far above the optimum pH) then there are too many OH- ions which- similarily to the H+ ions in too acidic solutions- then go on to interact with the ionic and hydrogen bonds in the enzymes tertiary structure, causing the bonds to break and the enzymes active site consequently changes and becomes permanently denatured.
    This, or if the pH is still below 7 but above optimum, there is simply less H+ ions than what is needed for the protein to interact with to maintain its desired shape.
 
 
 
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