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If the stability of numerous proteins or protein variations needs to be determined, substantial necessary protein production may be required. Here we now have determined the stability of acyl-coenzyme A binding protein at pH 5.3 and chymotrypsin inhibitor 2 at pH 3 and pH 6.25 by combined heat and denaturant unfolding. We utilized a setup where tryptophan fluorescence is measured in quartz capillaries where only 10 μl is required. Temperature unfolding of a series of 15 samples