Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves.

@article{Zweifel2002RelationshipsBT,
  title={Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves.},
  author={Mark E Zweifel and Doug Barrick},
  journal={Biophysical chemistry},
  year={2002},
  volume={101-102},
  pages={221-37}
}
We have used a simple binding model to consider how the thermodynamics of denaturant-protein interactions might influence the shape of protein stability curves (free energy change as a function of temperature), and how these effects translate into a temperature dependence of the apparent m-value (sensitivity of unfolding free energy to denaturant). We find that for an exothermic binding reaction with no binding heat capacity increment, increasing denaturant concentrations produces an apparent… CONTINUE READING

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