We report a direct current transport study of the local intergrain connections in a polycrystalline SmFeAsO 0.85 (Sm1111) bulk, for which we earlier estimated significant intergranular critical current density J c . Our combined low temperature laser scanning microscopy (LTLSM) and scanning electron microscopy observations revealed only few grain-to-grain transport current paths, most of which switched off when a magnetic field was applied. These regions typically occur where current crosses Fe-As, which is a normal-metal wetting-phase that surrounds Sm1111 grains, producing a dense array of superconducting-normal-superconducting contacts. Our study points out the need to reduce the amount of grain boundary-wetting Fe-As phase, as well as the crack density within pnictide grains, as these defects produce a multiply connected current-blocking network.

Current approaches aimed at determining the free energy surface of all-atom medium-size proteins in explicit solvent are slow and are not sufficient to converge to equilibrium properties. To ensure a proper sampling of the configurational space, it is preferable to use reduced representations such as implicit solvent and/or coarsegrained protein models, which are much lighter computationally. Each model must be verified, however, to ensure that it can recover experimental structures and thermodynamics. Here we test the coarse-grained implicit solvent OPEP model with replica exchange molecular dynamics (REMD) on six peptides ranging in length from 10 to 28 residues: two alanine-based peptides, the second -hairpin from protein G, the Trp-cage and zinc-finger motif, and a dimer of a coiled coil peptide. We show that REMD-OPEP recovers the proper thermodynamics of the systems studied, with accurate structural description of the -hairpin and Trp-cage peptides (within 1-2 Å from experiments). The light computational burden of REMD-OPEP, which enables us to generate many hundred nanoseconds at each temperature and fully assess convergence to equilibrium ensemble, opens the door to the determination of the free energy surface of larger proteins and assemblies.

We demonstrate that dopamine is able to self-polymerize and adhere firmly onto the substrate, which can create a hierarchical structure comprising an ultrathin active layer and a porous support layer. Such an approach opens a novel way to fabricating highly efficient and stable composite materials including composite membranes. More specifically, in this study the composite membranes are fabricated by simply dipping microporous substrate in aqueous dopamine solution under mild conditions. Nanoindentation measurement reveals the tight adhesion of dopamine onto microporous substrate, which is ascribed to numerous pi-pi and hydrogen-bonding interactions. The chemical composition of the active layer is analyzed by XPS, which demonstrates the self-polymerization of dopamine. The water contact angle of the dopamine coated membranes is reduced remarkably compared with that of the uncoated counterpart. Stylus profiler measurements display that the poly(dopamine) thickness increases as the coating time increases. FESEM images of the membranes' cross section show that an active layer (<100 nm) is deposited on the porous polysulfone (PS) substrate. Positron annihilation spectroscopy (PAS) is introduced to probe the fractional free volume properties throughout the cross section of the composite membranes and reveal that after dopamine double-coating the active layer becomes thicker and more compact. Moreover, pH and concentration of the dopamine solution exert notable influence on the fractional free volume of the composite membranes. The as-prepared membranes are tentatively employed for pervaporative desulfurization and exhibits satisfying separation performance as well as durability. This facile, versatile, and efficient approach enables a promising prospect for the wide applications of such novel kinds of ultrathin composite materials.

Self-assembly of the 40/42 amino acid A! peptide is a key player in Alzheimer's disease. A!40 is the most prevalent species, while A!42 is the most toxic. It has been suggested that the amino acids 21-30 could nucleate the folding of A! monomer and a bent in this region could be the rate-limiting step in A! fibril formation. In this study, we review our current understanding of the computer-predicted conformations of amino acids 23-28 in the monomer of A!(21-30) and the monomers A!40 and A!42. On the basis of new simulations on dimers of full-length A!, we propose that the ratelimiting step involves the formation of a multimeric !-sheet spanning the central hydrophobic core (residues 17-21).

High T c superconductivity in FeAs-based (pnictides) multilayers, evading temperature decoherence effects in a quantum condensate, is assigned to a Feshbach resonance (called also shape resonance) in the exchange-like interband pairing. The resonance is switched on by tuning the chemical potential at an electronic topological transition (ETT) near a band edge, where the Fermi surface topology of one of the subbands changes from 1D to 2D topology. We show that the tuning is realized by changing i) the misfit strain between the superconducting planes and the spacers ii) the charge density and iii) the disorder. The system is at the verge of a catastrophe i.e. near a structural and magnetic phase transition associated with the stripes (analogous to the 1/8 stripe phase in cuprates) order to disorder phase transition. Fine tuning of both the chemical potential and the disorder pushes the critical temperature T s of this phase transition to zero giving a quantum critical point. Here the quantum lattice and magnetic fluctuations promote the Feshbach resonance of the exchange-like anisotropic pairing. This superconducting phase that resists to the attacks of temperature is shown to be controlled by the interplay of the hopping energy between stripes and the quantum fluctuations. The superconducting gaps in the multiple Fermi surface spots reported by the recent ARPES experiment of D. V. Evtushinsky et al. arXiv:0809.4455 are shown to support the Feshbach scenario.

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The cytotoxicity of Alzheimer's disease has been linked to the self-assembly of the 4042 amino acid of the amyloid-beta (Abeta) peptide into oligomers. To understand the assembly process, it is important to characterize the very first steps of aggregation at an atomic level of detail. Here, we focus on the N-terminal fragment 1-28, known to form fibrils in vitro. Circular dichroism and NMR experiments indicate that the monomer of Abeta(1-28) is alpha-helical in a membranelike environment and random coil in aqueous solution. Using the activation-relaxation technique coupled with the OPEP coarse grained force field, we determine the structures of the monomer and of the dimer of Abeta(1-28). In agreement with experiments, we find that the monomer is predominantly random coil in character, but displays a non-negligible beta-strand probability in the N-terminal region. Dimerization impacts the structure of each chain and leads to an ensemble of intertwined conformations with little beta-strand content in the region Leu17-Ala21. All these structural characteristics are inconsistent with the amyloid fibril structure and indicate that the dimer has to undergo significant rearrangement en route to fibril formation.

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