Wrapping the cube and other polyhedra

An infinite series of twofold, two-way weavings of the cube, corresponding to 'wrappings', or double covers of the cube, is described with the aid of the two-parameter Goldberg- Coxeter construction. The strands of all such wrappings correspond to the central circuits (CCs) of octahedrites (four-regular polyhedral graphs with square and triangular faces), which for the cube necessarily have octahedral symmetry. Removing the symmetry constraint leads to wrappings of other eight-vertex convex polyhedra. Moreover, wrappings of convex polyhedra with fewer vertices can be generated by generalizing from octahedrites to i-hedrites, which additionally include digonal faces. When the strands of a wrapping correspond to the CCs of a four-regular graph that includes faces of size greater than 4, non-convex 'crinkled' wrappings are generated. The various generalizations have implications for activities as diverse as the construction of woven-closed baskets and the manufacture of advanced composite components of complex geometry. © 2012 The Royal Society.

Local Frustration Determines Molecular and Macroscopic Helix Structures

The effect of displaying cytochromes from an amyloid fibre is modelled as perturbation of -strands in a bilayer of helical -sheets, thereby explaining the spiral morphology of decorated amyloid and the dynamic response of morphology to cytochrome conformation. The morphology of the modelled fibre, which consists of minimal energy assemblies of rigid building blocks containing two anisotropic interacting units, depends primarily on the rigid constraints between units rather than the soft interactions between them. The framework is a discrete version of the bilayered frustration principle that drives morphology in Bauhinia seedpods. We show that self-assembly of frustrated long range structures can occur if the building blocks themselves are internally frustrated, e.g. amyloid morphology is governed by the conformation of the misfolded protein nucleating the fibre. Our model supports the idea that any peptide sequence can form amyloid if bilayers can form first, albeit stabilised by additional material such as chaperones or cytochromes. Analysis of experimentally derived amyloid structures supports our conclusions and suggests a range of frustration effects, which natural amyloid fibres may exploit. From this viewpoint, amyloid appears as a molecular example of a more general universal bilayered frustration principle, which may have profound implications for materials design using fibrous systems. Our model provides quantitative guidance for such applications. The relevance to longer length scales was proved by designing the morphology of a series of macroscopic magnetic stacks. Finally, this work leads to the idea of mixing controlled morphologically defined species to generate higher-order assembly and complex functional behaviour. The systematic kinking of decorated fibres and the nested frustration of the Bauhinia seed pod are two outstanding examples.