I am working with an oligomeric protein. I am using 9M urea to denature it but surprisingly when I do SDS PAGE of denatured protein i find a band of dimer and a monomer in the proportion 1:3 in intensity.
But when I do NMR of the denatured protein I get clear spectrum where all the amino acids are visible , which suggests that the protein is completely denatured ,i,e. there is no dimer present. This is very puzzling fro me.
What do you think can be reason for this?
Please give your suggestion on this.
Edited by sify, 20 June 2011 - 10:02 AM.