yes limited proteolysis is the best choice for the domain determination of
unknown protein from our lab some people did this. after doing
limited proteolysis just sequence digested part N terminally or the C
terminally and find out the region from where its getting digested.
side by side u can do
Dear all,
Thank you very much for all of information about domain determination! I
think the limited proteolysis is a good choice for the domain determination
as we have no information about a protein.
However, if we do have a domain information by the bioinformatics, how can
we truncate the do
for an experimental way to determine soluble domains see the following paper:
ESPRIT: an automated, library-based method for mapping and soluble expression
of protein domains from challenging targets.
Yumerefendi H, Tarendeau F, Mas PJ, Hart DJ.
J Struct Biol. 2010 Oct;172(1):66-74. Epub 2010 Mar
Hi,
To start with it would be great if you look in to the secondary structure
prediction of the sequence using any of the standard servers like PSIPRED,
JPRED etc. Many more available at expasy site http://ca.expasy.org/tools/.
Whatever construct you finally choose to make just remember the standar
Hi,
There's a whole bunch of programs that can help you "out there".
The 2 methods I think of right now are DISPROT (there's a server I
believe, http://www.ist.temple.edu/disprot/ ) - Must admit I haven't
been to that one for quite a while; DISPROT provides areas of your
sequence with high pro
Dear all,
Before we try to study the crystal structure of an unknown protein, we
need to determine the sequence that can fold into a compact and stable 3D
domain. What kinds of methods can we choose?
--
Best regards,
XH Wu
