Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
Nature, 1997•nature.com
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-β fold.
Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis,
and this may be relevant to amyloidosis generally.
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-β fold.
Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis,
and this may be relevant to amyloidosis generally.
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-β fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
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