Thermodynamic stability of wild-type and mutant p53 core domain.

@article{Bullock1997ThermodynamicSO,
  title={Thermodynamic stability of wild-type and mutant p53 core domain.},
  author={Alex N Bullock and J. F. or Henckel and Brian S. DeDecker and Christopher Johnson and Penka V. Nikolova and M. R. E. Proctor and David Philip Lane and A. R. Fersht},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 26},
  pages={
          14338-42
        }
}
Some 50% of human cancers are associated with mutations in the core domain of the tumor suppressor p53. Many mutations are thought just to destabilize the protein. To assess this and the possibility of rescue, we have set up a system to analyze the stability of the core domain and its mutants. The use of differential scanning calorimetry or spectroscopy to measure its melting temperature leads to irreversible denaturation and aggregation and so is useful as only a qualitative guide to stability… CONTINUE READING

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