10 December 2018 3 10K Report

Hi all,

I am working on a tricky protein. I surpassed some initial aggregation behaviour by adding 0.3% CHAPS and 1mM TCEP, buffer in which is happy until the removal of the SUMO tag, then it crashed out. When I spin the precipitate down and run the soluble fraction in SEC, my protein runs as a monomer. My question is: since the chaperone seems to be keeping it happy in solution, how far would you trust my soluble prep for activity assays? Do you think it would be correctly folded? Is it possible to have mixed populations of soluble, correctly folded protein and insoluble, misfolded one?

I don't wanna have high hopes on my monomeric protein, but still think it's worth giving it a shot in biochemical assays...

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