Expressing a tpeptide

Following my problems at reamplifying a full-length candidate gene I
am interested in, my boss suggested to amplify only a "portion" [2.5
KB cDNA] of it, containing all the conserved regions, and giving up on
the 3'end which is not really conserved.
The PCR was successfull, and before moving on the cloning and
expression steps of the work, I was wondering if this approach was
likely to be succesfull. I thought it was necessary to have the
complete gene sequence for a good folding of the encoded protein, and
an active heterologous protein. Does anybody have experience in this
domain?

In article <[Only registered users see links. ]> , [Only registered users see links. ] (Emilie) wrote:

One of the definitions of "protein domain" is "autonomous folding
unit". These are sometimes very hard to predict accurately.
Even if what you clone is a true individual domain of your protein,
it may not fold in E.coli (many possible reasons).

What your boss suggested is perfectly reasonable but if it
fails it means little.

DK