A friend of mine is getting ready to do some experiments involving purified human proteins expressed in E. coli, and she asked me if I knew anything about protein misfolding - apparently, proteins sometimes misfold when expressed in foreign vectors such as E. coli. Unfortunately, I didn't, but a Google search hit brought up an explanation that's really not that surprising when you think about it, and has to do with the fact that many proteins fold correctly only with the help of chaperone proteins or cofactors. Obviously, this can be a big problem for an experimentalist who wants to get usable amounts of a specific, correctly folded protein.
Does anyone know where to find good information about this problem or have suggestions for how to get around it (with or without changing vectors - I'm not sure if E.coli is a crucial part of the study or not)? The document I linked has some solutions but I'm wondering if there are any resources or "easy" tips out there I can forward along.