I don't care if the protein conformation or biological activity is lost. I just want to change Asn and Gln to Asp and Glu. I do want to avoid proteolysis.
These articles may be helpful:
http://pubs.acs.org/doi/abs/10.1021/jf00074a014?journalCode=jafcau
http://www.tandfonline.com/doi/abs/10.1080/10408399409527664
The change in protein structure will be drastic because Asn and Gln have opposite polarities from Asp and Glu. The deamination might even denature the protein so that its ability to form 3D structure is lost. Then of course, it depends on the protein - whether it has many or few Asn and Gln residues involved in H-bonding interactions. What specific scientific question are you trying to ask and solve by brute-force deamination? Site-directed mutagenesis to change specific Asn to Asp or Gln to Glu one at a time might be a better approach. A quick and dirty experiment is seldom worth the effort.
@Adam B Shapiro
The second link you provided was just what I needed. Thanks!
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