Conductance distributions in quasi-one-dimensional disordered wires

A detailed analysis of the distribution of conductances P(g) of quasi-one-dimensional disordered wires in the metal-insulator crossover is presented. P(g) obtained from a Monte Carlo solution of the Dorokhov, Mello, Pereyra, and Kumar (DMPK) scaling equation is in full agreement with "tight-binding" numerical calculations of bulk disordered wires. Perturbation theory is shown to be valid even for mean dimensionless conductances of the order of 1. In the crossover regime <, similar 1, P(g) presents a sharp feature at g=1 which is different from that observed in surface disordered wires.     

Investigation on a “tentacle-like” corrosion feature on Bronze Age tin-bronze objects

Studying the micro-structure of Austrian, Bosnian and Croatian Bronze Age objects made of tin bronze, a rare kind of corrosion feature, called in the following “tentacle-like” according to its specific way of penetrating the metallic matrix, was noted and investigated. Differing from the more classical intergranular, pitting, or crevice corrosion features, the “tentacle-like” corrosion is not following the grain boundaries, nor precisely positioned under the etching area, but penetrates mainly the crystal matrix without any apparent order. This paper discusses the first results achieved and the following hypotheses formulated in respect of the typology of this corrosion. The analyses were carried out by optical microscopy, Raman microspectroscopy, and scanning electron microscopy equipped with EDX spectroscopy for quantitative analyses.     

SSRL structural molecular biology summer school 2004

Exciting opportunities for early science at the National Synchrotron Light Source II (NSLS-II) drew over 260 participants to a workshop at Brookhaven National Laboratory, August 12–13, 2013. NSLS users planning to continue their work at the new facility joined prospective NSLS-II users to hear talks and debate possible research projects, beginning the process of creating a pool of experiment proposals and forming research teams.     

X‐ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin‐Coupled Molybdenum(III) Center

Nitrogenase enzymes catalyze the reduction of atmospheric dinitrogen to ammonia utilizing a Mo‐7Fe‐9S‐C active site, the so‐called FeMoco cluster. FeMoco and an analogous small‐molecule (Et₄N)[(Tp)MoFe₃S₄Cl₃] cubane have both been proposed to contain unusual spin‐coupled Mo^III sites with an S(Mo)=1/2 non‐Hund configuration at the Mo atom. Herein, we present Fe and Mo L₃‐edge X‐ray magnetic circular dichroism (XMCD) spectroscopy of the (Et₄N)[(Tp)MoFe₃S₄Cl₃] cubane and Fe L_2,3‐edge XMCD spectroscopy of the MoFe protein (containing both FeMoco and the 8Fe‐7S P‐cluster active sites). As the P‐clusters of MoFe protein have an S=0 total spin, these are effectively XMCD‐silent at low temperature and high magnetic field, allowing for FeMoco to be selectively probed by Fe L_2,3‐edge XMCD within the intact MoFe protein. Further, Mo L₃‐edge XMCD spectroscopy of the cubane model has provided experimental support for a local S(Mo)=1/2 configuration, demonstrating the power and selectivity of XMCD.     

Gold nanoparticles stabilized by modified halloysite nanotubes for catalytic applications

A highly sustainable prototype of a flow system based on gold nanoparticles (4.2 nm) supported on thiol‐functionalized halloysite nanotubes (HNTs) was developed for catalytic applications. The catalytic performances were evaluated using the reduction of 4‐nitrophenol to 4‐aminophenol as a model system. Under the best experimental conditions (0.0001 mol%, 1.97 × 10^?8 mg of Au nanoparticles), an impressive apparent turnover frequency value up to 2 204 530 h^?1 was achieved and the halloysite‐based catalyst showed full recyclability even after ten cycles. The high catalytic activity confirms the importance of the use of HNTs as support for Au nanoparticles that can exert a synergistic effect both as medium for transfer of electrons from borohydride ions to 4‐nitrophenol and by modulating interfacial electron transfer dynamics. With the application of flow technology, the obtained heterogeneous HNT@Au catalyst was fully recovered and reused for at least one month.     

Selective Targeting of Dendritic Cell‐Specific Intercellular Adhesion Molecule‐3‐Grabbing Nonintegrin (DC‐SIGN) with Mannose‐Based Glycomimetics: Synthesis and Interaction Studies of Bis(benzylamide) Derivatives of a Pseudomannobioside

Dendritic cell‐specific intercellular adhesion molecule‐3‐grabbing nonintegrin (DC‐SIGN) and Langerin are C‐type lectins of dendritic cells (DCs) that share a specificity for mannose and are involved in pathogen recognition. HIV is known to use DC‐SIGN on DCs to facilitate transinfection of T‐cells. Langerin, on the contrary, contributes to virus elimination; therefore, the inhibition of this latter receptor is undesired. Glycomimetic molecules targeting DC‐SIGN have been reported as promising agents for the inhibition of viral infections and for the modulation of immune responses mediated by DC‐SIGN. We show here for the first time that glycomimetics based on a mannose anchor can be tuned to selectively inhibit DC‐SIGN over Langerin. Based on structural and binding studies of a mannobioside mimic previously described by us ( 2 ), a focused library of derivatives was designed. The optimized synthesis gave fast and efficient access to a group of bis(amides), decorated with an azide‐terminated tether allowing further conjugation. SPR inhibition tests showed improvements over the parent pseudomannobioside by a factor of 3–4. A dimeric, macrocyclic structure ( 11 ) was also serendipitously obtained, which afforded a 30‐fold gain over the starting compound ( 2 ). The same ligands were tested against Langerin and found to exhibit high selectivity towards DC‐SIGN. Structural studies using saturation transfer difference NMR spectroscopy (STD‐NMR) were performed to analyze the binding mode of one representative library member with DC‐SIGN. Despite the overlap of some signals, it was established that the new ligand interacts with the protein in the same fashion as the parent pseudodisaccharide. The two aromatic amide moieties showed relatively high saturation in the STD spectrum, which suggests that the improved potency of the bis(amides) over the parent dimethyl ester can be attributed to lipophilic interactions between the aromatic groups of the ligand and the binding site of DC‐SIGN.     

Exploring Multi-Subsite Binding Pockets in Proteins: DEEP-STD NMR Fingerprinting and Molecular Dynamics Unveil a Cryptic Subsite at the GM1 Binding Pocket of Cholera Toxin B

Ligand-based NMR techniques to study protein–ligand interactions are potent tools in drug design. Saturation transfer difference (STD) NMR spectroscopy stands out as one of the most versatile techniques, allowing screening of fragments libraries and providing structural information on binding modes. Recently, it has been shown that a multi-frequency STD NMR approach, differential epitope mapping (DEEP)-STD NMR, can provide additional information on the orientation of small ligands within the binding pocket. Here, the approach is extended to a so-called DEEP-STD NMR fingerprinting technique to explore the binding subsites of cholera toxin subunit B (CTB). To that aim, the synthesis of a set of new ligands is presented, which have been subject to a thorough study of their interactions with CTB by weak affinity chromatography (WAC) and NMR spectroscopy. Remarkably, the combination of DEEP-STD NMR fingerprinting and Hamiltonian replica exchange molecular dynamics has proved to be an excellent approach to explore the geometry, flexibility, and ligand occupancy of multi-subsite binding pockets. In the particular case of CTB, it allowed the existence of a hitherto unknown binding subsite adjacent to the GM1 binding pocket to be revealed, paving the way to the design of novel leads for inhibition of this relevant toxin.