When orders of worth clash: Negotiating legitimacy in situations of moral multiplexity

How is moral legitimacy established in pluralist contexts where multiple moral frameworks co-exist and compete? Situations of moral multiplexity complicate not only whether an organization or practice is legitimate but also which criteria should be used to establish moral legitimacy. We argue that moral legitimacy can be thought of as the property of a dynamic dialogical process in which relations between moral schemes are constantly (re-)negotiated through dynamic exchange with audiences. Drawing on Boltanski and Thévenot's 'orders of worth' framework, we propose a process model of how three types of truces may be negotiated: transcendence, compromise, antagonism. While each can create moral legitimacy in pluralistic contexts, legitimacy is not a binary variable but varying in degrees of scope and certainty

Mutually orthogonal latin squares with large holes

Two latin squares are orthogonal if, when they are superimposed, every ordered pair of symbols appears exactly once. This definition extends naturally to `incomplete' latin squares each having a hole on the same rows, columns, and symbols. If an incomplete latin square of order $n$ has a hole of order $m$, then it is an easy observation that $n \ge 2m$. More generally, if a set of $t$ incomplete mutually orthogonal latin squares of order $n$ have a common hole of order $m$, then $n \ge (t+1)m$. In this article, we prove such sets of incomplete squares exist for all $n,m \gg 0$ satisfying $n \ge 8(t+1)^2 m$

Silica nanowires templated by amyloid-like fibrils

Many peptides self-assemble to form amyloid fibrils. We previously explored the sequence propensity to form amyloid using variants of a designed peptide with sequence KFFEAAAKKFFE. These variant peptides form highly stable amyloid fibrils with varied lateral assembly and are ideal to template further assembly of non-proteinaceous material. Herein, we show that the fibrils formed by peptide variants can be coated with a layer of silica to produce silica nanowires using tetraethyl-orthosilicate. The resulting nanowires were characterized using electron microscopy (TEM), X-ray fiber diffraction, FTIR and cross-section EM to reveal a nanostructure with peptidic core. Lysine residues play a role in templating the formation of silica on the fibril surface and, using this library of peptides, we have explored the contributions of lysine as well as arginine to silica templating, and find that sequence plays an important role in determining the physical nature and structure of the resulting nanowires