Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 386, Issue 3, Pages 869-877Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.11.005
Keywords
amyloid; neurodegeneration; prion; protein folding; structure
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Funding
- BioFuture grant
- Bundesministerium fur Bildung und Forschung
- Studienstiftung des deutschen Volkes
- EMBO
- National Institutes of Health [1 P01 GM-62580]
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Amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer's disease, Creutzfeldt-Jakob and type II diabetes. Alzheimer's amyloid fibrils consist of amyloid-beta (A beta) peptide and occur in a range of structurally different fibril morphologies. The structural characteristics of 12 single A beta(1-40) amyloid fibrils, all formed under the same solution conditions, were determined by electron cryo-microscopy and three-dimensional reconstruction. The majority of analyzed fibrils form a range of morphologies that show almost continuously altering structural properties. The observed fibril polymorphism implies that amyloid formation can lead, for the same polypeptide sequence, to many different patterns of inter- or intra-residue interactions. This property differs significantly from native, monomeric protein folding reactions that produce, for one protein sequence, only one ordered conformation an Only one set of inter-residue interactions. (c) 2008 Elsevier Ltd. All rights reserved.
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