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Atomic structure and hierarchical assembly of a cross-β amyloid fibril

Fitzpatrick, AW; Debelouchina, GT; Bayro, MJ; Clare, DK; Caporini, MA; Bajaj, VS; Jaroniec, CP; ... Dobson, CM; + view all (2013) Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proceedings of the National Academy of Sciences of the United States of America , 110 (14) pp. 5468-5473. 10.1073/pnas.1219476110. Gold open access

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Abstract

The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins into amyloid structures is linked to many debilitating human diseases, including several common forms of age-related dementia. Despite their importance, however, cross-β amyloid fibrils have proved to be recalcitrant to detailed structural analysis. By combining structural constraints from a series of experimental techniques spanning five orders of magnitude in length scale--including magic angle spinning nuclear magnetic resonance spectroscopy, X-ray fiber diffraction, cryoelectron microscopy, scanning transmission electron microscopy, and atomic force microscopy--we report the atomic-resolution (0.5 Å) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent β-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils.

Type: Article
Title: Atomic structure and hierarchical assembly of a cross-β amyloid fibril
Location: United States
Open access status: An open access publication
DOI: 10.1073/pnas.1219476110
Publisher version: http://dx.doi.org/10.1073/pnas.1219476110
Language: English
Additional information: Copyright © 2013 National Academy of Sciences.
Keywords: Amyloid, Cryoelectron Microscopy, Magnetic Resonance Spectroscopy, Microscopy, Electron, Scanning Transmission, Models, Molecular, Protein Structure, Secondary, X-Ray Diffraction
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1390327
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