Hi guys,

 

I was wondering about the feasibility of combining two domains from different proteins together. What sort of results can i expect? How often would I end up with a fully functioning protein?

 

I'm thinking about giving a non-specific enzyme with a domain that allows endonucleases that cut specifically

I think you're going to have to be a little more specific.

 

I was wondering about the feasibility of combining two domains from different proteins together. What sort of results can i expect? How often would I end up with a fully functioning protein?

You would expect for the two domains to be localized together/physically attached, and possibly for them to interfere with one anothers ability to function properly.

 

What do you mean by fully functioning?

 

Combining domains is done fairly commonly. Usually for the purpose of the addition of reporter domains to tag proteins e.g. GFP/YFP/RFP/CFP tags; or to assist in the purification/export of proteins by the addition of localization signals, his tags etc... It is often usefully to attach a domain of a protein that is exported out of a cell to assits in purification.

 

Assuming the modification doesn't interfere with the folding of the protein one can expect a functional protein.

 

Now all these really achieve is the localization of two elements together. Creation of new function by the combination of domains on the other hand isn't very likley. (Rational attempts at engineering new functions have proven very futile)

 

I'm thinking about giving a non-specific enzyme with a domain that allows endonucleases that cut specifically

 

I'm sorry I can't understand what you're trying to say, could you please reword this. (I can interpret this too many ways after making gramatical corrections.)