that was just idea, since I know, that proteins are sometimes extracted with the use of urea and then refolded during dialysis. But with the acidic environment it should work as well. Slowly increasing pH and the protein could refold.
i asked the same question to my bio teacher, and apparently there is no possibility that denatured protein can be fixed, unless someone have found something to fix the denatured protein
It will depend on the protein. If it is capable of spontaneous folding, it will probably refold when environment returns to normal. If it needs chaperones to help it fold, it would not refold. Ex: water soluble proteins are more likely to refold than membrane proteins.