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    What would happen if I have 1ml of pure protein, Then I add some arbitrary amount of acid, for example 0.1ml 1M HCl?
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    Would it not cause the protein to be 'denatured' - which would however only really be affected if some kind of enzyme, perhaps pepsin, was present?

    By the way, I'm not a chemist so don't take my word for it, I am kind of testing myself here and awaiting other replies to correct me

    Have you actually looked anything up on this topic, digestion, for example?
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    As above, you would disrupt the folding/bonding in the protein causing it to be denatured. The tolerance to acid is going to depend on the particular protein, though.
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    Will there be any chemical changes to the protein?? I'm doing western blot on a protein of interest, and having it denatured isn't a big deal (or is it?)
    By chemical changes, I mean changes to he amino acid structures and stuff like that.
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    There are likely to be chemical changes to the protein. If the protein makes up an enzyme, then the active site would probably be denatured. (Most likely it'll changes shape in some way). Hence, the enzyme cannot attach itself on to the substrate molecule.

    If its just a "normal" protein, there are likely to be chemical changes. Some ion may displace the Hydrogen out of the acid.
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    Well, it would alter hydrogen bonds so it would denature anything biological that does not operate at the given pH.
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    It may alter the local and net charges on the molecule? :shrug:
 
 
 
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