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-Structure paper
Title | Physical basis of amyloid fibril polymorphism. |
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Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 699, Year 2018 |
Publish date | Feb 16, 2018 |
Authors | William Close / Matthias Neumann / Andreas Schmidt / Manuel Hora / Karthikeyan Annamalai / Matthias Schmidt / Bernd Reif / Volker Schmidt / Nikolaus Grigorieff / Marcus Fändrich / |
PubMed Abstract | Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based ...Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangement of a structurally conserved building block. A comparison with the theoretically possible constellations reveals the experimentally observed spectrum of fibril morphologies to be governed by opposing sets of forces that primarily arise from the β-sheet twist, as well as peptide-peptide interactions within the fibril cross-section. Our results provide a framework for rationalizing and predicting the structure and polymorphism of cross-β fibrils, and suggest that a small number of physical parameters control the observed fibril architectures. |
External links | Nat Commun / PubMed:29453354 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 8.4 - 20.3 Å |
Structure data | EMDB-3986: EMDB-3987: EMDB-3988: EMDB-3989: EMDB-3990: EMDB-3991: EMDB-3992: EMDB-3993: EMDB-3994: |
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