I have induced a mutation of cysteine to arginine in a zinc finger motif of a protein. However rather than a missense mutation that was expected the mutation lead to generation of truncated protein. So, can I proceed further for biophysical characterisation of the mutant?
Most likely, the mutation you introduced leads to instability of the protein and subsequent truncation. If your goal was to study the effect of the point mutation, this seems compromised indeed. You may wish to study the truncated protein, but this is another story.
As others said, whether or not you study the truncated protein is your choice depending on what questions you are asking.
I'd sequence your expression vector to make sure that you have ONLY the one missence mutation. I'm guessing you have a frameshift that lead to the truncation.
Dear Shubhashish
did you checke the insert sequence to be sure that as Katie suggest you do not have a frameshift?
is this the only Cys, predicted to be a catalitic cys or are there other cys and is it possible that it is involved in a S-S bond and that the mutation produce protein instability and degradation during the culture?
As the others, i think that is not usefull characterize the truncated version but undertand why it is happen can help you to produce a non truncated one, or desing a new mutant to acheive the same result.
ciao
Manuele
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