Filled skutterudites are one of the most promising thermoelectric materials for power generation applications. The choice and concentration of filler atoms are key aspects for achieving high thermoelectric figure of merit values. We report on the high temperature thermoelectric properties in the double-filled skutterudites BaxYbyCo4Sb12. The combination of Ba and Yb fillers inside the voids of the skutterudite structure provides a broad range of resonant phonon scattering and consequently a strong suppression in the lattice thermal conductivity is observed. A dimensionless thermoelectric figure of merit of 1.36 at 800K is achievable for n-type BaxYbyCo4Sb12.

A family of proteases called caspases mediate apoptosis signaling in animals. We report a GFPbased fluorogenic protease reporter, dubbed "FlipGFP", by flipping a beta strand of the GFP. Upon protease activation and cleavage, the beta strand is restored, leading to reconstitution of the GFP and fluorescence. FlipGFP-based TEV protease reporter achieves 100-fold fluorescence change. A FlipGFP-based executioner caspase reporter visualized apoptosis in live zebrafish embryos with spatiotemporal resolution. FlipGFP also visualized apoptotic cells in the midgut of Drosophila.Thus, the FlipGFP-based caspase reporter will be useful for monitoring apoptosis during animal development and for designing reporters of proteases beyond caspases. The design strategy can be further applied to a red fluorescent protein for engineering a red fluorogenic protease reporter.

Amyloids adopt 'cross-β' structures composed of long, twisted fibrils with β-strands running perpendicular to the fibril axis. Recently, a toxic peptide was proposed to form amyloid-like cross-α structures in solution, with a planar bilayer-like assembly observed in the crystal structure. Here we crystallographically characterize designed peptides that assemble into spiraling cross-α amyloid-like structures, which resemble twisted β-amyloid fibrils. The peptides form helical dimers, stabilized by packing of small and apolar residues, and the dimers further assemble into cross-α amyloid-like fibrils with superhelical pitches ranging from 170 Å to 200 Å. When a small residue that appeared critical for packing was converted to leucine, it resulted in structural rearrangement to a helical polymer. Fluorescently tagged versions of the designed peptides form puncta in mammalian cells, which recover from photobleaching with markedly different kinetics. These structural folds could be potentially useful for directing in vivo protein assemblies with predetermined spacing and stabilities.

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U-box E3 ubiquitin ligases play important roles in the ubiquitin/26S proteasome machinery and in abiotic stress responses. TaPUB1-overexpressing wheat (Triticum aestivum L.) were generated to evaluate its function in salt tolerance. These plants had more salt stress tolerance during seedling and flowering stages, whereas the TaPUB1-RNA interference (RNAi)-mediated knock-down transgenic wheat showed more salt stress sensitivity than the wild type (WT). TaPUB1 overexpression upregulated the expression of genes related to ion channels and increased the net root Na + efflux, but decreased the net K + efflux and H + influx, thereby maintaining a low cytosolic Na + /K + ratio, compared with the WT. However, RNAi-mediated knock-down plants showed the opposite response to salt stress. TaPUB1 could induce the expression of some genes that improved the antioxidant capacity of plants under salt stress. TaPUB1 also interacted with TaMP (Triticum aestivum α-mannosidase protein), a regulator playing an important role in salt response in yeast and in plants. Thus, low cytosolic Na + / K + ratios and better antioxidant enzyme activities could be maintained in wheat with overexpression of TaPUB1 under salt stress. Therefore, we conclude that the U-box E3 ubiquitin ligase TaPUB1 positively regulates salt stress tolerance in wheat.

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