In Liquid Plasma for Surface Engineering of Cu Electrodes with Incorporated SiO2 Nanoparticles From Micro to Nano

A robust and efficient route to modify the chemical and physical properties of polycrystalline copper Cu wires via versatile plasma electrolysis is presented. Silica SiO2 nanoparticles 11 nm are introduced during the electrolysis to tailor the surface structure of the Cu electrode. The influence of these SiO2 nanoparticles on the structure of the Cu electrodes during plasma electrolysis over a wide array of applied voltages and processing time is investigated systematically. Homogeneously distributed 3D coral like microstructures are observed by scanning electron microscopy on the Cu surface after the in liquid plasma treatment. These 3D microstructures grow with increasing plasma processing time. Interestingly, the microstructured copper electrode is composed of CuO as a thin outer layer and a significant amount of inner Cu2O. Furthermore, the oxide film thickness between 1 and 70 m , the surface morphology, and the chemical composition can be tuned by controlling the plasma parameters. Remarkably, the fabricated microstructures can be transformed to nanospheres assembled in coral like microstructures by a simple electrochemical treatmen

Optical Sum Rule in Finite Bands

In a single finite electronic band the total optical spectral weight or optical sum carries information on the interactions involved between the charge carriers as well as on their band structure. It varies with temperature as well as with impurity scattering. The single band optical sum also bears some relationship to the charge carrier kinetic energy and, thus, can potentially provide useful information, particularly on its change as the charge carriers go from normal to superconducting state. Here we review the considerable advances that have recently been made in the context of high $T_c$ oxides, both theoretical and experimental.Comment: Review article accepted for publication in J. Low Temp. Phys. 29 pages, 33 figure

Hsp90^.Cdc37 complexes with protein kinases form cooperatively with multiple distinct interaction sites.

Protein kinases are the most prominent group of heat shock protein 90 (Hsp90) clients and are recruited to the molecular chaperone by the kinase-specific cochaperone cell division cycle 37 (Cdc37). The interaction between Hsp90 and nematode Cdc37 is mediated by binding of the Hsp90 middle domain to an N-terminal region of Caenorhabditis elegans Cdc37 (CeCdc37). Here we map the binding site by NMR spectroscopy and define amino acids relevant for the interaction between CeCdc37 and the middle domain of Hsp90. Apart from these distinct Cdc37/ Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes. In both cases, the C-terminal part of Cdc37 is relevant for kinase binding, whereas the N-terminal domain displaces the nucleotide from the kinase. This interaction leads to a cooperative formation of the ternary complex of Cdc37 and kinase with Hsp90. For the mitogen-activated protein kinase extracellular signalregulated kinase 2 (Erk2), we observe that certain features of the interaction with Cdc37.Hsp90 are conserved, but the contribution of Cdc37 domains varies slightly, implying that different kinases may utilize distinct variations of this binding mode to interact with the Hsp90 chaperone machinery

Thinking outside the gate: Single-cell assessments in multiple dimensions.

Experimental cancer immunology and therap