A little update on my own project:
It is a secreted protein without any modification reported. Size exclusion shows that it is an oligomer. CD spectrum shows well-defined secondary structure.
It is stable and soluble.
It may have different states in diseases' condition.
Now I was trying to figure out the native state of this protein. As told by folks on CCP4bb, Most likely, the bacterial expression reveals its original state.
Am I right?
Thanks a lot,
Jerry
Date: Fri, 28 May 2010 11:40:31 -0700
From:
[log in to unmask]Subject: [ccp4bb] to what extent bacterial expression reveals the native oligomerization state of mammalian proteins.
To:
[log in to unmask]Dear ALL:
I am sorry for this stupid question.
I guess bacterial expression system is still most popular in structural biology.
If you get a very good soluble E.coli expression of a human protein without disulfide bonds,
to what extent do you believe that the oligomerization state of this bacterial expression will reflect the real physiological state of this protein in humans?
Can someone give comments or refer some literature?
Thanks a lot,
Jerry McCully
Hotmail has tools for the New Busy. Search, chat and e-mail from your inbox.
Learn more.
The New Busy is not the old busy. Search, chat and e-mail from your inbox.
Get started.