Guanidine-induced unfolding of the Sso7d protein from the hyperthermophilic archaeon Sulfolobus solfataricus

International Journal of Biological Macromolecules
Vincenzo GranataG Graziano

Abstract

The unfolding induced by guanidine hydrochloride of the small protein Sso7d from the hyperthermophilic archaeon Sulfolobus solfataricus has been investigated by means of circular dichroism and fluorescence measurements. At neutral pH and room temperature the midpoint of the transition occurred at 4M guanidine hydrochloride. Thermodynamic information was obtained by means of both the linear extrapolation model and the denaturant binding model, in the assumption of a two-state N<==>D transition. A comparison with thermodynamic data determined from the thermal unfolding of Sso7d indicated that the denaturant binding model has to be preferred. Finally, it is shown that Sso7d is the most stable against both temperature and guanidine hydrochloride among a set of globular proteins possessing a very similar 3D structure.

References

Jul 11, 1995·Biochemistry·I M Plaza del Pino, J M Sanchez-Ruiz
Feb 24, 2000·Biopolymers·A J SaundersD A Erie
Mar 16, 2001·Trends in Biotechnology·J M Sanchez-Ruiz, G I Makhatadze
Sep 12, 2001·Trends in Biochemical Sciences·A Karshikoff, R Ladenstein

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Citations

Jan 24, 2007·Proteins·Giovanni RenzoneAnnamaria Guagliardi
Dec 10, 2015·International Journal of Biological Macromolecules·Ajit KumarAdemola O Olaniran

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