Elucidation of the mechanism of globular protein folding is a major issue in structural biology, and recent progress in the experimental studies on protein folding has improved understanding of transient structural intermediates along the folding pathway. Recent excellent techniques have shown the presence of he intermediate at an early stage of folding, which has the native-like secondary structure in the same regions as those in the native molecule and the destroyed specific tertiary structure. Also, these intermediates have been shown to be identical with the molten globule (MG) state observed for some proteins such as alpha -lactalbumin ( alpha -LA) as a compact equilibrium unfolding intermediate.
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