Hi everyone,

I am trying to find a cheap way to compare the proteomic composition and abundance of some bone samples. In particular, I am expecting to see a reduction in the abundance of some of these proteins as a result of different treatments that I will perform on these bones.

Since I have to exclude HPLC/MS-MS (too expensive) and any other mass spectrometry technique, and since I believe that an SDS page will results in a complex smear (more than 50-60 proteins in the mixture) and a 2D-GE will be too complicated to find differences between my samples, I was thinking to simply quantify my samples in order to compare them. But, since I am expecting some proteins within this mixture being more denatured in same samples than in others, my question is: are protein assays (e.g., Bradford, BCA, etc.) able to provide different quantification results for denatured vs folded proteins? I don't know exactly the chemistry behind them, so anyone able to help me will be extremely appreciated! Any other suggestion will be appreciated as well!

Many thanks!

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