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

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

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, o...

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Detalles Bibliográficos
Autores principales: Booth, DR, Sunde, M, Bellotti, V, Robinson, C, Hutchinson, W, Fraser, P, Hawkins, P, Dobson, C, Radford, SE, Blake, C, Pepys, M
Formato: Journal article
Lenguaje:English
Publicado: 1997

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