I have my samples out of which few dissolve in THF and few in DMSO. I want to do interaction study of these compounds with model protein like Bovine Serum Albumin. Upto what percentage of these solvents, the protein structure will remain unaltered or does not get denatured?
If anyone can also give me some article links pertaining to this, it would be still more helpful.
By 40% DMSO, BSA undergoes denaturation. You can refer the article Chemphyschem. 2013 Aug 5;14(11):2441-9 for details.
In more general terms, should you consider other proteins, the stability of the structure is obviously case specific but up to 2% of DMSO is usually considered a safe concentration level of DMSO
You'll need to measure it for your particular case. Most of my enzyme assays see ~10% inhibition when using 2% DMSO. Carrier concentrations is something you should validate for yourself by measuring the different levels of response in your assay with different concentrations of solvent.
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