Axially symmetric Einstein-Straus models

The existence of static and axially symmetric regions in a Friedman-Lemaitre cosmology is investigated under the only assumption that the cosmic time and the static time match properly on the boundary hypersurface. It turns out that the most general form for the static region is a two-sphere with arbitrarily changing radius which moves along the axis of symmetry in a determined way. The geometry of the interior region is completely determined in terms of background objects. When any of the most widely used energy-momentum contents for the interior region is imposed, both the interior geometry and the shape of the static region must become exactly spherically symmetric. This shows that the Einstein-Straus model, which is the generally accepted answer for the null influence of the cosmic expansion on the local physics, is not a robust model and it is rather an exceptional and isolated situation. Hence, its suitability for solving the interplay between cosmic expansion and local physics is doubtful and more adequate models should be investigated.Comment: Latex, no figure

Free-Trade Ideology and Transatlantic Abolitionism: A Historiography

Copyright © The History of Economics Society 2015. Author's accepted version deposited in accordance with SHERPA RoMEO guidelines. The definitive version is available at http://dx.doi.org/10.1017/S1053837215000103.This essay seeks to trace the many—and often conflicting—economic ideological interpretations of the transatlantic abolitionist impulse. In particular, it explores the contested relationship between free-trade ideology and transatlantic abolitionism, and highlights the understudied influence of Victorian free-trade ideology within the American abolitionist movement. By bringing together historiographical controversies from the American and British side, the essay calls into question long-standing conceptions regarding the relationship between free trade and abolitionism, and suggests new avenues for research

Reconstruction of cellular variability from spatiotemporal patterns of Dictyostelium discoideum

Variability in cell properties can be an important driving mechanism behind spatiotemporal patterns in biological systems, as the degree of cell-to-cell differences determines the capacity of cells to locally synchronize and, consequently, form patterns on a larger spatial scale. In principle, certain features of spatial patterns emerging with time may be regulated by variability or, more specifically, by certain constellations of cell-to-cell differences. Similarly, measuring variability in a system (i.e. the spatial distribution of cell-cell differences) may help predict properties of later-stage patterns

Structural Analysis of Papain-Like NlpC/P60 Superfamily Enzymes with a Circularly Permuted Topology Reveals Potential Lipid Binding Sites

NlpC/P60 superfamily papain-like enzymes play important roles in all kingdoms of life. Two members of this superfamily, LRAT-like and YaeF/YiiX-like families, were predicted to contain a catalytic domain that is circularly permuted such that the catalytic cysteine is located near the C-terminus, instead of at the N-terminus. These permuted enzymes are widespread in virus, pathogenic bacteria, and eukaryotes. We determined the crystal structure of a member of the YaeF/YiiX-like family from Bacillus cereus in complex with lysine. The structure, which adopts a ligand-induced, “closed” conformation, confirms the circular permutation of catalytic residues. A comparative analysis of other related protein structures within the NlpC/P60 superfamily is presented. Permutated NlpC/P60 enzymes contain a similar conserved core and arrangement of catalytic residues, including a Cys/His-containing triad and an additional conserved tyrosine. More surprisingly, permuted enzymes have a hydrophobic S1 binding pocket that is distinct from previously characterized enzymes in the family, indicative of novel substrate specificity. Further analysis of a structural homolog, YiiX (PDB 2if6) identified a fatty acid in the conserved hydrophobic pocket, thus providing additional insights into possible function of these novel enzymes