Mutational analysis of the propensity for amyloid formation by a globular protein

@article{Chiti2000MutationalAO,
  title={Mutational analysis of the propensity for amyloid formation by a globular protein},
  author={F. Chiti and N. Taddei and M. Bucciantini and P. White and G. Ramponi and C. Dobson},
  journal={The EMBO Journal},
  year={2000},
  volume={19}
}
Acylphosphatase can be converted in vitro, by addition of trifluoroethanol (TFE), into amyloid fibrils of the type observed in a range of human diseases. The propensity to form fibrils has been investigated for a series of mutants of acylphosphatase by monitoring the range of TFE concentrations that result in aggregation. We have found that the tendency to aggregate correlates inversely with the conformational stability of the native state of the protein in the different mutants. In accord with… Expand
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Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
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