Coupled Folding and Binding of the Disordered Protein PUMA Does Not Require Particular Residual Structure

@inproceedings{Rogers2014CoupledFA,
  title={Coupled
Folding and Binding of the Disordered Protein
PUMA Does Not Require Particular Residual Structure},
  author={Joseph M. Rogers and Chi Tat Wong and Jane Clarke},
  booktitle={Journal of the American Chemical Society},
  year={2014}
}
Many cellular proteins are 'disordered' in isolation. A subset of these intrinsically disordered proteins (IDPs) can, upon binding another molecule, fold to a well-defined three-dimensional structure. In the structurally heterogeneous, unbound ensemble of these IDPs, conformations are likely to exist that, in part, resemble the final bound form. It has been suggested that these conformations, displaying 'residual structure', could be important for the mechanism of such coupled folding and… CONTINUE READING

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Biochemistry

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