Thousands of proteins likely to have long disordered regions.

@article{Romero1998ThousandsOP,
  title={Thousands of proteins likely to have long disordered regions.},
  author={Pedro Rafael Matheus Romero and Zoran Obradovic and Charles Kissinger and J. Ernest Villafranca and Ethan Garner and S D Guilliot and A. Keith Dunker},
  journal={Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing},
  year={1998},
  pages={
          437-48
        }
}
Neural network predictors of protein disorder using primary sequence information were developed and applied to the Swiss Protein Database. More than 15,000 proteins were predicted to contain disordered regions of at least 40 consecutive amino acids, with more than 1,000 having especially high scores indicating disorder. These results support proposals that consideration of structure-activity relationships in proteins need to be broadened to include unfolded or disordered protein. 

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