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EC Number pH Stability pH Stability Maximum Commentary Reference
Show all pathways known for 1.1.1.145Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1454.5 7.4 circular dichroism shows that between pH 7.4 and 4.5, 3betaHSD2 retains its primarily alpha-helical character with a decrease in beta-helical content at lower pH values, whereas the beta-sheet content remains unchanged throughout. Titrating the pH back to 7.4 restores the original conformation 725511
Show all pathways known for 1.1.1.145Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.1454.5 7.4 incubation with guanidinum hydrochloride shows a three-step cooperative unfolding of 3betaHSD2 from pH 7.4 to 4.5. With further decreases in pH, increasing concentrations of GdmHCl lead to rapid two-step unfolding that may represent complete loss of structure. Between pH 4 and 5, the two intermediate states appear stable. Stopped-flow kinetics show slower unfolding at around pH 4, where the protein is in a pseudostable state. At pH 4-5, 3betaHSD2 takes on a molten globule conformation that promotes the dual functionality of the enzyme 725511
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