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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.

Original publication

DOI

10.1038/385787a0

Type

Journal article

Journal

Nature

Publication Date

27/02/1997

Volume

385

Pages

787 - 793

Keywords

Amyloid, Amyloidosis, Circular Dichroism, Cloning, Molecular, Crystallography, X-Ray, Enzyme Stability, Hot Temperature, Humans, Liver Diseases, Models, Molecular, Muramidase, Point Mutation, Protein Conformation, Protein Denaturation, Protein Folding, Protein Structure, Secondary, Recombinant Proteins