I am working on expressing two separate proteins (domains) in E. coli to avoid the challenges associated with expressing a single large protein (83 Kda). These proteins do not naturally form a complex, but I aim to assemble them into a functional heterodimeric structure after purification.
Since they will not be co-expressed, I am looking for effective strategies to facilitate their correct assembly post-expression.
What are the best experimental techniques to ensure proper folding and interaction
Any insights or references to similar studies would be greatly appreciated!
An 83 Kda protein is on the large side but is certainly not extremely large. Have you tried the native protein first, it might work fine and save you the problem of trying to assemble your final protein from fragments.
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