Hi fellow researchers,

I am trying to purify a protein of 50KDa for structure function analysis and folding unfolding kinetics using chemical denaturant. I have purified my protein from Inclusion bodies and found purity level as shown in SDS-PAGE attached below after purification and refolding.

Is these fractions are good enough to go for circular dichroism and fluoroscence spectroscopy based studies? What is the purification level needed to perform such studies on a protein?

Fraction-1 is unfolded purified fraction and all others are purified folded fractions.

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