Which is the best method to recover a precipitated protein back into its normally folded state?
Don’t really understand the question. Is that a list of possible answer choices or are they the different situations that caused the protein to precipitate? Getting a precipitated protein to refold is a multi-step procedure. I’m not familiar with using any of those chemicals. Maybe if I give you my general reasoning process, it will help you figure it out. The first thing I would do is resolubilize the precipitate. I would try a solution with a high concentration of urea first. If that didn’t work, I would try guanidine. If that didn’t work, I don’t know what I would use. Detergents might get the protein solubilized again, but they are a royal pain in the *** to get rid of afterwards, so I would only consider them as a last resort. I might try some sort of organic solvent, but that is starting to get a little crazy. You could add a little heat as well. You might need a reducing agent if there are disulfide bridges present. After the protein is solubilized in its denatured form, the nex
