Dear all:
I have expressed my peptide, a truncated fragment of a protein, in
insoluble form, then I refolded it into water soluble peptide. The
expressed product was fused to GST. I could not detect any GST activity
in the refold protein, but tryptic digestion of the refolded protein
gave an trypsin resistance fragment as the tryptic digestion of the
native protein.
I do not know that the tryptic resistance fragment have the same
conformation as the one from the tryptic digestion of the native
protein. It was not successful to isolate the trypsin resistance
fragment from the native protein under non-denaturing condition ;that
is why I have to express this part of peptide.
Anyone would please give me general criterion to determind whether the
refolded protein
adopted the propered conformation? Any suggestion and comment are
welcome.
Thanks you in advance for your reply.
Jongrak
--
-----------------------------------Mr. Jongrak Kittiworakarn
g3937506 at student.mahidol.ac.th
Inst. of Science and Technology for Research and Development
Mahidol University (Salaya Campus)
Salaya, Nokornprathom, THAILAND.
Tel. 001-66-2-441-9003-7 ext.1277,1278,1279
Fax. 001-66-2-441-9906, 001-66-2-441-1013
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