The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways.

@article{Kelly1998TheAC,
  title={The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways.},
  author={Jeffery W Kelly},
  journal={Current opinion in structural biology},
  year={1998},
  volume={8 1},
  pages={101-6}
}
The conformational change hypothesis postulates that tertiary structural changes under partially denaturing conditions convert one of 17 normally soluble and functional human proteins into an alternative conformation that subsequently undergoes self-assembly into an amyloid fibril, the putative causative agent in amyloid disease. This hypothesis is consistent with Anfinsen's view that the tertiary structure of a protein is determined both by its sequence and the aqueous environment; the latter… CONTINUE READING

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