Hi Xiaopeng
To add to Artem's comments:
Does the presumed gsh make a mixed disulfide in the active site?i.e. is it
covalently bonded to the active site via a s-s bond?
If yes then MS on your purified sample should easily give you the answer.
If a mixed s-s is indeed the scenario then purifying the
Tightly bound ligands commonly survive purification :) Several unexpected
discoveries have been made this way!
If you think your stuff is GSH, soak some 'real' GSH or co-crystallize with
it, and see if density shape changes from what you had before. This is not
guaranteed to work because sometimes
Dear all,
Sorry for this off topic question.
We are working on protein/inhibitor complex structure although we can not get
our inhibitors in. However, we did find a strange density at the active site,
it looks really like GSH, the natural co-enzyme of thiis protein.We tried to
use very simple
