Two-orbit switch-pitch structures

The Hoberman 'switch-pitch ' ball is a transformable structure with a single folding and unfolding path. The underlying cubic structure has a novel mechanism that retains tetrahedral symmetry during folding. Here, we propose a generalized class of structures of a similar type that retain their full symmetry during folding. The key idea is that we require two orbits of nodes for the structure: within each orbit, any node can be copied to any other node by a symmetry operation. Each member is connected to two nodes, which may be in different orbits, by revolute joints. We will describe the symmetry analysis that reveals the symmetry of the internal mechanism modes for a switch-pitch structure. To follow the complete folding path of the structure, a nonlinear iterative predictor-corrector algorithm based on the Newton method is adopted. First, a simple tetrahedral example of the class of two-orbit structures is presented. Typical configurations along the folding path are shown. Larger members of the class of structures are also presented, all with cubic symmetry. These switch-pitch structures could have useful applications as deployable structures.

An organizing center in a planar model of neuronal excitability

This paper studies the excitability properties of a generalized FitzHugh-Nagumo model. The model differs from the classical FitzHugh-Nagumo model in that it accounts for the effect of cooperative gating variables such as activation of calcium currents. Excitability is explored by unfolding a pitchfork bifurcation that is shown to organize five different types of excitability. In addition to the three classical types of neuronal excitability, two novel types are described and distinctly associated to the presence of cooperative variables. © 2012 Society for Industrial and Applied Mathematics.

Fibers with integrated mechanochemical switches: minimalistic design principles derived from fibronectin.

Inspired by molecular mechanisms that cells exploit to sense mechanical forces and convert them into biochemical signals, chemists dream of designing mechanochemical switches integrated into materials. Using the adhesion protein fibronectin, whose multiple repeats essentially display distinct molecular recognition motifs, we derived a computational model to explain how minimalistic designs of repeats translate into the mechanical characteristics of their fibrillar assemblies. The hierarchy of repeat-unfolding within fibrils is controlled not only by their relative mechanical stabilities, as found for single molecules, but also by the strength of cryptic interactions between adjacent molecules that become activated by stretching. The force-induced exposure of cryptic sites furthermore regulates the nonlinearity of stress-strain curves, the strain at which such fibers break, and the refolding kinetics and fraction of misfolded repeats. Gaining such computational insights at the mesoscale is important because translating protein-based concepts into novel polymer designs has proven difficult.