FUN!!!!!
pH refers to the presence of hydronium ions and hydroxide ions (it goes into more detail, but that is the jist of it). These ions cause changes in other molecules based on there localised
pKa (akin to pH) values.
Protiens are constructed of amino acids in a peptide chain via peptide bonds. The order of these amino acids determines the overall structure of the protien. There are primary (the order of the amino acids), secondary (weather or not these orders form alpha helix or beta pleated sheet or non-form strands), tertiary (how the secondary structres interact and form shapes of the protiens), and quatranary (how the lumps of tertiary structrues fit together) stuctrues of all protiens.
All of these protiens (with the exception of cystine, which forms a disulfide bond) form hydrogen bonds with all of the end groups on the amino acids in the protien chain. pH will effect these interactions quite drasicly. pH allows the presence of H3O+ or OH- ions in solution, which can very easily overide hydrogen bonding, and change bonds themselves. Going outside of a protiens "active pH range" will cause it usually to denature. Denaturing of a protein means that it unwinds and just forms a squiggly spagetti noodle of a strand that largely does nothing. pH can can also cause the conformational change of a protien as well, changing the charge of ionic amino acids such as histidine. I could go on but I think I am getting long-winded
In a nutshell pH changes the protien stucture and can render it active or inactive.
I am going to run to dinner, but if you have any more questions, ask away!