Display Settings:


Send to:

Choose Destination
Nature. 1997 Feb 27;385(6619):787-93.

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

Author information

  • 1Immunological Medicine Unit, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK.


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.

Comment in

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Icon for Nature Publishing Group
    Loading ...
    Write to the Help Desk