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Transient formation...
Abstract
Ämnesord
Stäng
- During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the A-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended -strand conformation.
Nyckelord
- peptide aggregation
- protein aggregation
- amyloid fibrils
- peptide crystal
- electron microscopy
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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