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Form Factor of Helical Ribbons

DOI: 10.1021/ma8014917 DOI Help

Authors: Ian Hamley (University of Reading; Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Macromolecules , VOL 41 (22) , PAGES 8948-8950

State: Published (Approved)
Published: October 2008

Abstract: The misfolding of proteins and peptides can lead to fibrillar aggregates which are often termed amyloid fibrils. These are characterized by a cross-beta structure, with -strands and polypeptide backbones running perpendicular to the fibril axis, which is coincident with the hydrogen bonding direction. Several types of amyloid fibrils have been shown by high resolution electron microscopy to comprise assemblies of individual twisted -sheets,2-5 of which there are two typesstapes or ribbons. The two are distinguished by the presence or absence of a hollow core in the fibril. The twist arises from packing constraints of the side groups of the residues within the beta-Strands.

Subject Areas: Biology and Bio-materials

Technical Areas: