Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
| Autor: | Vittorio Bellotti, Sheena E. Radford, Winston L. Hutchinson, Mark B. Pepys, Colin C.F. Blake, Paul E. Fraser, Carol V. Robinson, Christopher M. Dobson, Philip N. Hawkins, Margaret Sunde, David R. Booth |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Amyloid Protein Denaturation Protein Folding Circular dichroism Hot Temperature Protein Conformation macromolecular substances Crystallography X-Ray Fibril Protein Structure Secondary chemistry.chemical_compound Protein structure Enzyme Stability medicine Humans Point Mutation Cloning Molecular chemistry.chemical_classification Multidisciplinary Chemistry Circular Dichroism Liver Diseases Amyloidosis Fibrillogenesis medicine.disease Recombinant Proteins Biochemistry Muramidase Protein folding Lysozyme Glycoprotein |
| Zdroj: | Nature. 385:787-793 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/385787a0 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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