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.