Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

@article{Jackson1991FoldingOC,
  title={Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.},
  author={Sophie E. Jackson and A. R. Fersht},
  journal={Biochemistry},
  year={1991},
  volume={30 43},
  pages={10428-35}
}
The reversible folding and unfolding of barley chymotrypsin inhibitor 2 (CI2) appears to be a rare example in which both equilibria and kinetics are described by a two-state model. Equilibrium denaturation by guanidinium chloride and heat is completely reversible, and the data can be fitted to a simple two-state model involving only native and denatured forms. The free energy of folding in the absence of denaturant, delta GH2O, at pH 6.3, is calculated to be 7.03 +/- 0.16 and 7.18 +/- 0.43 kcal… CONTINUE READING
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