In article <38gocl$l4d at mark.ucdavis.edu>,
George Theodoris <ez003450 at bullwinkle.ucdavis.edu> wrote:
>Colin Rasmussen (ras-1 at bones.biochem.ualberta.ca) wrote:
>> Perhaps fusing it to GAL4 will disrupt the
>confirmation, rendering it unable to interact with whatever proteins it
The problem is that you get into an infinite regression here. Even if your
protein has activity when fused to Gal4(minus NLS), that doesn't
make any guarantee about when it is fused to normal GAl4.
It's actually probably simpler, less time-consuming, and more
straightforward to just make the GAL4 fusion, and screen for your
interacting factors. It may not be worth spending time to prove that it
might work when you can spend the same time doing the actual experiment.
If you identify a factor, then you will have hosts of experiments to do
depending on what the factor is. At this point, it is unlikely that anyone
will want to know if your original contruct was in it's proper conformation.
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