I made several combinations of mutations in a 747 amino acid-protein based on prediction tool as well as some additional mutations in non-predicted lysines including one affecting all 42 lysine of the protein. I did not observe a phenotypic change specific to K-R mutation, but I think the effect of fluorescent tag used here is more dominant in the protein stability. I am wondering if anyone has also observed the effect of changes in amino acid side chain geometry and electrostatic interactions in such R variants.
I suggest you contact David Vukovic at the University of Zürich. He is a late-stage PhD student doing a very comprehensive study on the factors influencing ubiquitin-dependent protein degradation as well as the pitfalls inherent in various methods to quantify protein degradation. I just heard one of his excellent talks, and verified that it is OK for me to redirect research gate questions to him.
Annemarie Honegger Thank you for your suggestion! I appreciate it. Hopefully David Vukovic will be able to provide me specific answer.
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