Think about this: based on the contents of different solutions, more/less salt or higher/lower pH, proteins will be either folded (referred to as the proper conformational shape or conformation) or unfolded / denatured. This is because while proteins fold due to internal molecular interactions like hydrogen bonds, a large portion of protein folding has to do with the hydrophobic nature of different amino groups. As the solution changes, so do the hydration shells around the polypeptides and each cell is going to have its own unique internal chemistry.
When it comes to your question it's important to remember that it isn't as simple as just inserting DNA to a cell to get the protein created. Polypeptide chains are often processed through the endoplasmic reticulum, or the Golgi, where they pick up and lose things like disulfide bonds, cell pathway signals, or just help folding to find stable hydrogen bonds.
Protein signaling is pretty complex stuff, and studying the processing of proteins is difficult work. But, it's important to remember that bacteria have been making all the medical insulin on the planet since before either of us was born - so it can be done.
-SG
Not necessarily different cells within a single organism, but say you were to splice a really large protein from a Human into a bacteria or the other way around (or any animal or plant or fungus, etc) - when the cell goes to synthesize that protein would it be likely to fold differently? "Likely" meaning "will it fold differently within that cell type more often than it might misfold otherwise."--If there is a difference in the way proteins are folded between different types of cells, is there any relatively comprehensive list of the differences and members of different groups of protein folding/misfolding mechanics?
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