Journal of Molecular Biology -
1 days and 23 hours ago
Publication Date: 2008 Nov 14 PMID: 19038266br/Authors: Meinhardt, J. - Sachse, C. - Hortschansky,
P. - Grigorieff, N. - Fandrich, M.br/Journal: J Mol Biolbr/br/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 (Abeta) peptide and occur in a range
of structurally different fibril morphologies. The structural characteristics of 12 single
Abeta(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 and only one set of inter-residue interactions.br/br/post
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