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Is it possible to mutate a region of a protein (says about 300 amino acids long) without actually mutating the gene?

One possible way that I can think of is to use RNAi and specifically block that region of the mRNA which codes for the 300 amino acids in the protein?

But then wouldn't it cause a problem in the translation of the remaining region of the protein?

Are there any methods out there to mutate a region of a protein without mutating the DNA?

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    $\begingroup$ "One possible way that I can think of is to use RNAi and specifically block that region of the mRna which codes for the 300 amino acids in the protein?".... Not possible. RNAi doesn't work that way. $\endgroup$ – WYSIWYG May 27 '16 at 11:46
  • $\begingroup$ Maybe there is a chemical to make error during translation by ribosoms. $\endgroup$ – Reyhaneh S Jun 1 '16 at 16:12
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I assume that you mean changing the amino acid sequence in a single protein in an organism to one that no longer reflects the sequence predicted from the DNA sequence. In that case, I would suggest using ADAR (Double-stranded RNA-specific adenosine deaminase) or similar enzymes. ADAR deaminates adenosine to inosine, which is read by the ribosome as a guanine. I know that it's activity is regulated, but I'm not sure how you could redirect it (perhaps with an antisense RNA that yields a double-stranded binding stretch in the target RNA.

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To a certain extent, maybe. However RNAi would not work as you describe because it causes the whold mRNA to be degraded not just a portion of it.

If the gene in question is spliced, you could probably influence the splicing pattern by triggering certain signalling pathways. But this is limited to producing different splicing variants of your gene and is likely equally or more difficult than mutating the actual gene.

Another alternative would be to produce mutated mRNA and inject/transform/transfec that into the cell in question but again this is likely as difficult or more difficult than mutating the gene.

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