The stability of a protein is a basic feature that controls whether or not the protein is functional under certain conditions. Equilibrium unfolding with denaturants necessitates many sample preparations and only gives the free energy of folding when performed at a single temperature. The usual protein requirement for a sample is 0.5–1 mg. If the stability of a large number of proteins or protein variations needs to be assessed, large amounts of protein may be required. Using of a combination of temperature and denaturant unfolding to test the stability of acylcoenzyme a binding protein at pH 5.3 and chymotrypsin inhibitor 2 at pH 3 and pH 6.25.
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