ZnO composite nanolayer with mobility edge quantization for multi-value logic transistors.

A quantum confined transport based on a zinc oxide composite nanolayer that has conducting states with mobility edge quantization is proposed and was applied to develop multi-value logic transistors with stable intermediate states. A composite nanolayer with zinc oxide quantum dots embedded in amorphous zinc oxide domains generated quantized conducting states at the mobility edge, which we refer to as "mobility edge quantization". The unique quantized conducting state effectively restricted the occupied number of carriers due to its low density of states, which enable current saturation.

Single-Crystal Poly[4-(4,4-dihexadecyl-4H-cyclopenta[1,2-b:5,4-b']dithiophen-2-yl)- alt-[1,2,5]thiadiazolo[3,4- c]pyridine] Nanowires with Ultrahigh Mobility.

We fabricated single-crystal poly[4-(4,4-dihexadecyl-4H-cyclopenta[1,2-b:5,4-b']-dithiophen-2-yl)- alt-[1,2,5]thiadiazolo-[3,4- c]pyridine] (PCDTPT) nanowires with ultrahigh mobility using a liquid-bridge-mediated nanotransfer molding method. The structural analysis of the single-crystal PCDTPT nanowires reveals that PCDTPT crystals have a triclinic structure, and the nanowires grow parallel to PCDTPT backbone chains, which provide important insights into its intrinsic charge transport. The single-crystal PCDTPT nanowire exhibits a superior charge carrier mobility of 72.

The dependence of nano-contact magnetoresistance on the bulk scattering spin asymmetry in CoFe alloys with oxidation impurities.

Nano-contact magnetoresistance (NCMR) spin-valves (SVs) using an AlO nano-oxide-layer (NOL) have numerous nanocontacts in the thin AlO oxide layer. The NCMR theoretically depends on the bulk scattering spin asymmetry ([Formula: see text]) of the ferromagnetic material in the nanocontacts. To determine the relationship between NCMR and [Formula: see text], we investigated the dependence of NCMR on the composition of the ferromagnetic material CoFe.

Electromyographic activity of the masseter muscle after radiofrequency therapy in an animal model.

Purpose: The purpose of this study was to examine changes in the electromyographic (EMG) activity of the masseter muscle after radiofrequency therapy (RF).

Methods: Twelve rabbits were used in this study: four in each group according to the number of RF applications. Preoperative EMG in the masseter muscle was used as the control.

The change in dimension of the masseter muscle in rabbits after radiofrequency therapy.

Purpose: The objective of this study was to evaluate the change in muscle dimension after administering radiofrequency (RF) therapy.

Materials And Methods: This study used 6 male New Zealand rabbits. Groups were divided by number of applications of RF (eg, 1 to 4 points).

The solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum: a structural homolog of the FF domain.

The ribosomal protein S17E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. S17E is a 62-residue protein conserved in archaea and eukaryotes and has no counterparts in bacteria. Mammalian S17E is a phosphoprotein component of eukaryotic ribosomes.

Lys296 and Arg299 residues in the C-terminus of MD-ACO1 are essential for a 1-aminocyclopropane-1-carboxylate oxidase enzyme activity.

The 1-aminocyclopropane-1-carboxylate (ACC) oxidase catalyzes the last step in the biosynthesis of ethylene from ACC in higher plants. The complex structure of ACC oxidase/Fe(2+)/H(2)O derived from Petunia hybrida has recently been established by X-ray crystallography and it provides a vast structural information for ACC oxidase. Our mutagenesis study shows that both Lys296 and Arg299 residues in the C-terminal helix play important roles in enzyme activity.

Solution structure of YKR049C, a putative redox protein from Saccharomyces cerevisiae.

YKR049C is a mitochondrial protein in Saccharomyces cerevisiae that is conserved among yeast species, including Candida albicans. However, no biological function for YKR049C has been ascribed based on its primary sequence information. In the present study, NMR spectroscopy was used to determine the putative biological function of YKR049C based on its solution structure.

Exploring protein fold space by secondary structure prediction using data distribution method on Grid platform.

Motivation: Since the newly developed Grid platform has been considered as a powerful tool to share resources in the Internet environment, it is of interest to demonstrate an efficient methodology to process massive biological data on the Grid environments at a low cost. This paper presents an efficient and economical method based on a Grid platform to predict secondary structures of all proteins in a given organism, which normally requires a long computation time through sequential execution, by means of processing a large amount of protein sequence data simultaneously. From the prediction results, a genome scale protein fold space can be pursued.

Solution structure of a novel calcium binding protein, MTH1880, from Methanobacterium thermoautotrophicum.

MTH1880 is a hypothetical protein from Methanobacterium thermoautotrophicum, a target organism of structural genomics. The solution structure determined by NMR spectroscopy demonstrates a typical alpha + beta-fold found in many proteins with different functions. The molecular surface of the protein reveals a small, highly acidic pocket comprising loop B (Asp36, Asp37, Asp38), the end of beta2 (Glu39), and loop D (Ser57, Ser58, Ser61), indicating that the protein would have a possible cation binding site.

Structure-based functional discovery of proteins: structural proteomics.

The discovery of biochemical and cellular functions of unannotated gene products begins with a database search of proteins with structure/sequence homologues based on known genes. Very recently, a number of frontier groups in structural biology proposed a new paradigm to predict biological functions of an unknown protein on the basis of its three-dimensional structure on a genomic scale. Structural proteomics (genomics), a research area for structure-based functional discovery, aims to complete the protein-folding universe of all gene products in a cell.

Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum.

The ribosomal protein S28E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. Sequence homologs of S28E are found only in archaea and eukaryotes. Here we report the three-dimensional solution structure of S28E by NMR spectroscopy.