Unstructured to structured transition of an intrinsically disordered protein peptide in coupling Ca²⁺-sensing and SK channel activation.

@article{Zhang2013UnstructuredTS,
  title={Unstructured to structured transition of an intrinsically disordered protein peptide in coupling Ca²⁺-sensing and SK channel activation.},
  author={Miao Zhang and John M. Pascal and Ji-fang Zhang},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 12},
  pages={4828-33}
}
Most proteins, such as ion channels, form well-organized 3D structures to carry out their specific functions. A typical voltage-gated potassium channel subunit has six transmembrane segments (S1-S6) to form the voltage-sensing domain and the pore domain. Conformational changes of these domains result in opening of the channel pore. Intrinsically disordered (ID) proteins/peptides are considered equally important for the protein functions. However, it is difficult to explore the structural… CONTINUE READING

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