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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.

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

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Publisher copy:
10.1038/385787a0

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
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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

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