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pH protein denaturation

Postby Miichawl » Mon Apr 15, 2019 2:30 am

Is there a difference between the denaturation of a protein when the pH levels are more acidic compared to more alkaline?

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Re: pH protein denaturation

Postby 17eugenekim » Mon Apr 15, 2019 9:43 am

I would say that depends on what scope you are looking at. From a chemistry standpoint, low vs high pH affects proteins differently. But in the context of a cell or an organism, pH denaturation in either direction has essentially the same result: the protein "unfolds" and stops working. The electrostatic (+ attracts –) forces that keep a protein folded in its proper conformation are degraded under acidic/basic environments, because those positive and negative charges can be changed and removed. In low pH, there are lots of protons (+) hanging around, so negative charges are neutralized; in high pH, there are less protons, or "more –OH" hanging around, so positive charges are neutralized. This is a bit of an oversimplification, but in the end, the result is the same - the protein doesn't hold up its shape, and it stops working like it needs to.

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