Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding.

@article{Verkhivker2003SimulatingDT,
  title={Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding.},
  author={Gennady M Verkhivker and Djamal Bouzida and Daniel K. Gehlhaar and Paul A. Rejto and Stephan T. Freer and Peter W. Rose},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 9},
  pages={5148-53}
}
A microscopic study of functional disorder-order folding transitions coupled to binding is performed for the p27 protein, which derives a kinetic advantage from the intrinsically disordered unbound form on binding with the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex. Hierarchy of structural loss during p27 coupled unfolding and unbinding is simulated by using high-temperature Monte Carlo simulations initiated from the crystal structure of the tertiary complex. Subsequent… CONTINUE READING

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