Fusion protein activity

Andrew Doherty A.Doherty at Bris.ac.uk
Fri Nov 8 03:40:46 EST 1996

slavemaster z wrote:
> In article <55ki8e$1lo at falcon.le.ac.uk>, EB15 at le.ac.uk says...
> >
> >> Are fusion protein usually active?
> >
> >To quote a well known politician: This question can be answered by a very
> >clear "That depends".
> >
> >In other words: Sometimes they are, some times they are not. No way of
> >predicting it either. Good luck
> >
> Not so, cleverle.
> from my personal experience & talking to a lot of hip froods
> acting in the field, I would estimate that at least 80% of all
> His tagged fushion proteins are as active as the wild type one.
> z
Yeah, but it also depends on the type of fusion you're making, how big
the reporter is in relation to the native protein, where you put the
reporter and whether any other accessory proteins are required for some
activities, which the reporter screws up. There is no way of predicting
what effect any fusion construction will have on the activity of the
native protein - it's still a very empirical "science". If 80% of His
tagged proteins are active, you still can't predict which ones are going
to be INactive. IMHO, if the reporter is small in relation to the native
protein, then you've a better chance of getting a functional fusion

Hope it helps

Andy D
Dr Andrew Doherty		email -  a.doherty at bris.ac.uk
Dept. Anatomy			Tel (0117)9287421
School of Medical Sciences	Fax (0117)9287402
University of Bristol
University Walk
Bristol UK

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