I have a protein that is expressed in inclusion bodies (E. coli expression) and I have solubilized it in 6 M GuHCl. I know different methods for protein refolding (dialysis, dilution or in column) and the possible use of several refolding conditions, such as pH and additives. I wonder where to start to optimize the refolding conditions. Eventually, it would be nice to go toward in column refolding as the protein has an His-tag.
There is another technique that is folding under pressure with devices such as a Barafold apparatus. See publications by Gary Powell and Bob Petrovich at NIEHS on researchgate.
I think the key for any system is to use refolding kits that provide various buffer compositions. To screen, the easiest way is by dilution or high pressure first with different buffers. If the protein is put in let's say ten different buffers, a simple spin procedure followed by SDS PAGE and protein concentration assay will tell you how much soluble protein is present. A functional assay is also extremely useful and important because sometimes while the protein is very soluble, it may not be refolded properly. Please see our paper on ADAM9 in researchgate. We used an activity assay with our protein to pick which conditions were best and this was done with high pressure. However, since most labs don't have a high pressure device, the same buffers were used to refold on a Ni NTA column, and it worked great.
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