Publisher: Bentham Science Publishers
E-ISSN: 1875-5305|13|6|545-547
ISSN: 0929-8665
Source: Protein and Peptide Letters, Vol.13, Iss.6, 2006-06, pp. : 545-547
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Abstract
The effect of methanol and trifluoroethanol (TFE) on the structure and folding of molten globule state of procerain, a cysteine protease from Calotropis procera, was studied by circular dichroism spectroscopy. The magnitude of ellipticity at 215 nm, as a measure of &bgr;-sheet content, is dependent on the concentration of the TFE. Interestingly, a switch over from the &bgr;-sheet structure of the molten globule state to &agr;-helix was observed at 60% TFE and the ellipticity at 222 nm increased as a function of TFE concentration beyond this critical TFE concentration. Temperature induced unfolding of the molten globule state of procerain in 10% methanol showed stabilization of &agr;-rich domain with concomitant destabilization of &bgr;-rich domain. Using higher concentration of methanol (20-40 %) had no stabilizing effect on the &agr;-rich domain however, the &bgr;-rich domain was destabilized, indicating that the stability of the domains were not interdependent and that a low concentration of methanol induced stabilization in &agr;-rich domain.
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