Abstract
Ovalbumin is an important member of the serpin superfamily without inhibitory activity. The heat- and pH-induced alpha-to-beta structural transformations of ovalbumin were investigated by means of circular dichroism and binding of ANS and Congo red dyes. The native ovalbumin shows a mixture of alpha-helix and beta-sheet, while both the heat and alkali treatments are able to transform the native protein into a predominance of beta-sheet secondary structure. The free energy changes during transitions to the unfolded state are 5.19 kcal/mol from the native state and 4.00 kcal/mol from the heat-treated one. The binding abilities of the heat-treated and the alkali-treated forms to ANS and Congo red suggest that the altered forms exhibit hydrophobic exposure and intermolecular interaction. The results substantiate that the altered protein forms bearing increased beta-sheet structures are prone to aggregation, which is implicated in the pathogenesis of some conformational diseases.
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