Dear Researchers,

My protein of interest has 30 cys residues in it. After refolding, all form disulfide bonds.

I performed Ellman's assay to detect the free thiol groups in the protein. The OD of the protein came 0.085 and that of blank is 0.08.

I took the Cysteine standards from 1.6mM to 0.00625mM (2 fold serial dilutions of standard)

I am finding difficulty in drawing any conclusion from my experiment. Does that mean all cys residues in my protein has formed disulfide bonds and none of the Cys residues is free?

Please help with the explanations as I need to give this data in my research soon.

Your inputs will be greatly appreciated.