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Abstract
The effect of denaturing (urea, guanidine hydrochloride (Gdn HCl)), and stabilizing (sucrose) media on the capacity of vicilin from fababeans to self-associate into a micelle arrangement was examined. The micelle observations were related to protein conformational parameters, specifically thermal stability plus aliphatic (CPA) and aromatic (ANS) surface hydrophobicity (S 0). Both urea and GdnHCl had a negative impact on micelle formation at low concentrations (0·1 m urea and 0·2 m GdnHCl). At higher denaturant levels, the deteriorating micelle response was correlated with a decrease in thermal stability (T d, ΔH) and a decrease in aromatic and aliphatic S 0 values. Exposure to sucrose was also detrimental to micelle formation; this was attributed to preferential hydration of the protein molecules. In all situations, a delicate balance of hydrophilic-hydrophobic forces seemed to be required for the micelle phenomenon.
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