Hi there,

What exactly are you interested in : theory of refolding itself or experimental approaches for an efficient refolding? About the second part of your quest : any non disordered protein exhibits a tertiary structure under it's native state so there are plenty of examples in literature.

I made a mistake!!! I've corrected my question. I'm looking for experimental approaches for refolding of proteins with quaternary structure. 

Hi again,

I think the following paper should be a good overview on the different strategies:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030991/

The article Dominique posted is very good (thank you) though it does not discuss the refolding of His-tagged proteins in 6M GuHCl on the column by using a step gradient, or linear gradient of buffer without GuHCl, in someways it is similar to the microfluidic chip refolding the authors discuss, but the His-tag media is cheap, widely available, and the process can be done on the bench using a lab-made column, or prepacked column, and a syringe to push the buffers through the column.

Hi Gary,

I thought about it actually but immobilization of denatured monomers may be a drawback for the final assembly step  into oligomers as the question is about quaternary structures.

Would you want to know about covalent and/or non-covalent  dimers with hetero and/or homo subunits as examples?  If you want a couple of simple examples from personal experience with many such systems then have a look at SCF(stem cell factor) and PDGF (platelet derived growth factor).  Refold systems for quat proteins usually do not involve detergents or solid phase approaches and usually have relatively longer total refold times.