A new method for determining the constant-pressure heat capacity change associated with the protein denaturation induced by guanidinium chloride (or urea)

Biophysical Chemistry
Ritu SinghFaizan Ahmad

Abstract

Differential scanning calorimetry (DSC) provides authentic and accurate value of DeltaC(p)(X), the constant-pressure heat capacity change associated with the N (native state)<-->X (heat denatured state), the heat-induced denaturation equilibrium of the protein in the absence of a chemical denaturant. If X retains native-like buried hydrophobic interaction, DeltaC(p)(X) must be less than DeltaC(p)(D), the constant-pressure heat capacity change associated with the transition, N<-->D, where the state D is not only more unfolded than X but it also has its all groups exposed to water. One problem is that for most proteins D is observed only in the presence of chemical denaturants such as guanidinium chloride (GdmCl) and urea. Another problem is that DSC cannot yield authentic DeltaC(p)(D), for its measurement invokes the existence of putative specific binding sites for the chemical denaturants on N and D. We have developed a non-calorimetric method for the measurements of DeltaC(p)(D), which uses thermodynamic data obtained from the isothermal GdmCl (or urea)-induced denaturation and heat-induced denaturation in the presence of the chemical denaturant concentration at which significant concentrations of both N and D exist. We show t...Continue Reading

References

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Citations

Jul 14, 2011·Journal of Molecular Neuroscience : MN·Xin LiBaoxue Yang
Jun 25, 2009·Journal of Biosciences·Laishram R SinghFaizan Ahmad
Dec 20, 2012·Journal of Biomolecular Structure & Dynamics·H Sepasi TehraniA A Saboury
Mar 4, 2009·Biochimica Et Biophysica Acta·Laishram R SinghFaizan Ahmad

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