- Abstract:
- Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
- Publication status:
- Published
- Publisher copy:
- 10.1038/385787a0
-
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- Journal:
- Nature
- Volume:
- 385
- Issue:
- 6619
- Pages:
- 787-793
- Publication date:
- 1997-02-05
- DOI:
- EISSN:
-
1476-4687
- ISSN:
-
0028-0836
- URN:
-
uuid:749cd3d2-a987-4109-b15b-88f8fead4e2c
- Source identifiers:
-
59432
- Local pid:
- pubs:59432
- Language:
- English
- Keywords:
- Copyright date:
- 1997
Journal article
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.
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