Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase.
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A structure-activity relationship study with a series of aldol substrates shows that the mechanism of the antibody 38C2-catalyzed retrograde aldol reaction depends on the nature of the substrate With electron-deficient substrates an early deprotonation precedes the C-C bond cleavage while with electron-rich substrates the catalytic mechanism involves an initial C-C bond cleavage leading to a positively charged intermediate.
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