Hi, Dear All,
Looks like I got a lot of aggregation problem and thanks a lot for all
the replies about last email.Now, I have another question.I have one
protein that is well-folded ( confirmed by 1D NMR ) and the CD spectrum
looks fine.But when I tried to do CD scans at different
temperatures(20C to 95C), I noticed that the protein forms aggregation
instead of unfolding at high temperature.( 95C ) and it's
non-reversible.Is that the intrinsic property of the sequence (maybe
some sequence are aggregation prone) or maybe something that I can
modify during purification? The pI of the protein is 6.2( with His
tag).Is there any way or any kind of experiment that I can try to
figure out why it aggregate? I assume the problem coming from the
sequence itself.
Thanks.
Jenny
