I am afraid that you might have your protein in an unfolded state and
thus, trapped by the chaperon At least this is what I have
experienced in the past... If the protein is properly folded but it
gets trapped by the chaperon due to hydrophobic interaction, washes
with ATP, Mg2+ and K+
We have had good luck with making a protein soluble using the Artic Express
bacterial cell line BUT we can't get rid of the chaperone that copurifies.
We have tried adding ATP, MgCl2 and potassium to lysate and extensive
washes and this releases a bit of the chaperone. Has anyone solved this
probl
