Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.

@article{Calamai2005AmyloidFF,
  title={Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.},
  author={Martino Calamai and Fabrizio Chiti and Christopher M. Dobson},
  journal={Biophysical journal},
  year={2005},
  volume={89 6},
  pages={4201-10}
}
Protein misfolding and aggregation are interconnected processes involved in a wide variety of nonneuropathic, systemic, and neurodegenerative diseases. More generally, if mutations in sequence or changes in environmental conditions lead to partial unfolding of the native state of a protein, it will often aggregate, sometimes into well-defined fibrillar structures. A great deal of interest has been directed at discovering the characteristic features of metastable partially unfolded states that… CONTINUE READING

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