Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis.

@article{Jackson1993StructureOT,
  title={Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis.},
  author={Sophie E. Jackson and N Elmasry and A. R. Fersht},
  journal={Biochemistry},
  year={1993},
  volume={32 42},
  pages={11270-8}
}
Chymotrypsin inhibitor 2 (CI2) unfolds and refolds according to a simple two-state kinetic mechanism. The single rate-determining transition state may thus be studied by kinetics of both unfolding and refolding. This has allowed the direct testing of some facets of the protein engineering procedure (phi-value analysis). The structure of the hydrophobic core of CI2 in the transition state was analyzed from kinetic and thermodynamic measurements of guanidinium chloride-induced unfolding of 11… CONTINUE READING
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