Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators.

@article{Marsh2010StructuralDI,
  title={Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators.},
  author={Joseph A. Marsh and Barbara Dancheck and Michael J Ragusa and Marc Allaire and Julie Deborah Forman-Kay and Wolfgang Peti},
  journal={Structure},
  year={2010},
  volume={18 9},
  pages={1094-103}
}
Complete folding is not a prerequisite for protein function, as disordered and partially folded states of proteins frequently perform essential biological functions. In order to understand their functions at the molecular level, we utilized diverse experimental measurements to calculate ensemble models of three nonhomologous, intrinsically disordered proteins: I-2, spinophilin, and DARPP-32, which bind to and regulate protein phosphatase 1 (PP1). The models demonstrate that these proteins have… CONTINUE READING

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