From protein sequence to dynamics and disorder with DynaMine.

@article{Cilia2013FromPS,
  title={From protein sequence to dynamics and disorder with DynaMine.},
  author={Elisa Cilia and Rita Pancsa and Peter Tompa and Tom Lenaerts and Wim F. Vranken},
  journal={Nature communications},
  year={2013},
  volume={4},
  pages={
          2741
        }
}
Protein function and dynamics are closely related; however, accurate dynamics information is difficult to obtain. Here based on a carefully assembled data set derived from experimental data for proteins in solution, we quantify backbone dynamics properties on the amino-acid level and develop DynaMine--a fast, high-quality predictor of protein backbone dynamics. DynaMine uses only protein sequence information as input and shows great potential in distinguishing regions of different structural… CONTINUE READING
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An assignment of intrinsically disordered regions of proteins based on NMR structures

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