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pH adjusting is necessary because it will create a favorable
environment which such substance, for instance enzyme, will work
properly.
For example, Tris-HCl should be adjusted into pH 7.5 to get the
optimal DNase and RNase activity in your assays.

What happens if we're to alter the pH. Does it mean that inductiion
and resonance does not operate efficiently rendering the protein in
question to cross fire all the electrophiles and nucleophiles in the
wrong order and sequences such tat we can get a more than active
enzyme?

This should be a very interesting question schould we be able to prove the theory above to be validable.

[sdekivit]

by altering the pH, the enzyme denatures and thus the spatial conformation of the enzyme changes. Because of this conformation difference, the to be converted molecule won't fit in the enzyme and the result is thus a less effective catalization.

An enzyme has a pH-value were activitiy is at its max. Enzymes have a so called optimum-curve, for both pH and temperature. For example pepsin is most active at pH = 2 but lipase however has its maximal activity at pH = 8.

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True.

But if you were to examine closely an enzyme, for example a 'modified' version of Serine Protease - alpha chymotrypsin - yo'd get to see that the lysine and arginine residue are side by side and do most of the activity for the enzyme, although you'd still need to take into account that very important activity coming from the aromatic ring electron donating and accepting alternating mechanism of the histine residue a few yards down the road, but nevertheless... almost right beside that lysine residue.

I'd take a closer look at what this histine is promising to do with its ' ;Don' and 'off' states.

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OK, so its not lysine and arginine - its aspartate and histidine and Serine is 'a few yards down the road'.

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pockets of a pocket of a pocket of a pocket.