Suppose we have a protein complex A, B, C where A interacts with B, but not with C, and C interacts with B, but not with A. What would be a reason why I can get the A,B,C complex from coexpression of those proteins in E.coli host, but not after incubating individual proteins together and running them on SEC chromatography?
One possibility is that the affinity of the proteins for each other is not high enough to maintain the interaction when the proteins are passed through the gel filtration resin.
Another possibility is that the interaction between the proteins occurs biosynthetically, i.e., during folding. When the proteins are prepared individually, the regions of interaction may not be available.
Probably... the formation of the complex could be formed by some kind of helper protein that holds the three proteins together and allows them to form a strong stable complex. If you incubate the three proteins without this extra helper or factor, then the complex would not be formed.
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