Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.

@article{Hilser2007IntrinsicDA,
  title={Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.},
  author={Vincent J. Hilser and E Brad Thompson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 20},
  pages={8311-5}
}
Transcription factors and other allosteric cell signaling proteins contain a disproportionate number of domains or segments that are intrinsically disordered (ID) under native conditions. In many cases folding of these segments is coupled to binding with one or more of their interaction partners, suggesting that intrinsic disorder plays an important functional role. Despite numerous hypotheses for the role of ID domains in regulation, a mechanistic model has yet to be established that can… CONTINUE READING