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A predominant conformational isomer of non-native α-lactalbumin (α-LA) has been purified by thermal denaturation of the native α-LA using the technique of disulfide scrambling. This unique isomer retains a substantial content of α-helical structure. It is stabilized by two native disulfide bonds within the α-helical domain and two scrambled non-native disulfide bonds at the β-sheet domain. This denatured...
In the presence of denaturant and thiol initiator, the native bovine pancreatic trypsin inhibitor (BPTI) denatures by shuffling its native disulfide bonds and converts to a mixture of scrambled isomers. The extent of denaturation is evaluated by the relative yields of the scrambled and native species of BPTI. BPTI is an exceedingly stable molecule and can be effectively denatured only by guanidine...
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