Off the top, I don't know the answer to this, but will note that
ammonium sulfate and urea have opposite effects on protein solubility
and water structure. Urea is a chaotrope that reduces the strength of
the hydrophobic effect--hence promoting protein unfolding. Ammonium
sulfate is a "kosmotrope" that strengthens the hydrophobic effect, and
protein precipitation is in part driven by increased protein-protein
association. So these two treatments would work against each other.
Detergents also reduce reduce hydrophobic association, but in a slightly
different manner. So what is it you are trying to accomplish? Protein
concentration? Protein refolding? Protein purification? There are
probably better alternatives than ammonium sulfate treatment.
_______________________________________
Roger S. Rowlett
Gordon & Dorothy Kline Professor
Department of Chemistry
Colgate University
13 Oak Drive
Hamilton, NY 13346
tel: (315)-228-7245
ofc: (315)-228-7395
fax: (315)-228-7935
email: rrowl...@colgate.edu
On 9/24/2012 12:52 PM, Koyeli Pramanik wrote:
Hi All,
My protein can be solubilized in 8M Urea or detergents. Could anyone
suggest me whether ammonium sulfate precipitation of my desired
protein works good for denaturing conditions?
Thanks a lot for your help!
Regards,
Koyeli
