Characterization and study of high conductivity antimony-doped tin oxide thin films grown by mist chemical vapor deposition.

Antimony doped tin oxide thin films are grown at atmospheric pressure using a home-built mist chemical vapor deposition system, which is an environmental-friendly technique with low energy consumption. For obtaining high quality Sb:SnO x films, different solutions are used to support the film fabrication process. The role of each component in supporting solution is also preliminarily analyzed and studied. In this work, the growth rate, density, transmittance, hall effect, conductivity, surface morphology, crystallinity, component and chemical states of Sb:SnO x films are investigated. Sb:SnO x films prepared at 400 °C using a mixing solution of H2O, HNO3 and HCl show a low electrical resistivity of 6.58 × 10-4 Ω cm, high carrier concentration of 3.26 × 1021 cm-3, high transmittance of 90%, and wide optical band gas of 4.22 eV. X-ray photoelectron spectroscopy analyses disclose that the samples with good properties have high [Sn4+]/[Sn2+] and [O-Sn4+]/[O-Sn2+] ratios. Moreover, it is discovered that supporting solutions also affect the CBM-VBM level and Fermi level in the band diagram of thin films. These experimental results confirm that Sb:SnO x films grown using mist CVD are a mixture of SnO2 and SnO. The sufficient supply of oxygen from supporting solutions leads to the stronger combination of cations and oxygen, and the combination of cations and impurities disappear, which is one of the reasons for obtaining high conductivity Sb:SnO x films.

Nightly fasting duration is not associated with the prevalence of metabolic syndrome among non-shift workers: The Furukawa Nutrition and Health Studymx.

OBJECTIVES: While several experimental studies in animals and humans have suggested the protective effect of nightly fasting duration (NFD) against cardiometabolic risk factors, few population-based studies have been conducted. This study aimed to investigate the association between NFD and metabolic syndrome (MetS) among Japanese non-shift workers. METHODS: A subset of 1054 non-shift workers from the Furukawa Nutrition and Health Study were included in this analysis. Participants completed dietary and lifestyle surveys during a periodic checkup. NFD was defined as the time between dinner and breakfast and was categorized into four groups (ie, ≥12 hours, 11 hours, 10 hours, and ≤9 hours). MetS was defined as ≥3 of the following components: high waist circumference (≥90 cm [men] and ≥80 cm [women]), high triglycerides (≥150 mg/dL), low high-density lipoprotein cholesterol (<40 mg/dL [men] and <50 mg/dL [women]), hypertension (systolic blood pressure ≥130 mm Hg or diastolic blood pressure ≥85 mm Hg), and high fasting glucose (fasting plasma glucose ≥100 mg/dL or hemoglobin A1c ≥5.6%). A multivariable logistic regression model was used to examine the association between NFD and MetS. RESULTS: The odds ratios (95% confidence intervals) of MetS for the highest (≥12 hours) through lowest (≤9 hours) NFD categories were 1.00 (reference), 0.83 (0.51-1.35), 0.83 (0.48-1.43), and 0.80 (0.43-1.48) (P for trend = 0.50) after adjusting for covariates. Further analyses on the relationship between NFD and each MetS component found no significant associations. CONCLUSIONS: We did not find any evidence of a significant association between NFD and MetS among non-shift workers in Japan.

Functional Role of Fibrillin5 in Acclimation to Photooxidative Stress.

The functional role of a lipid-associated soluble protein, fibrillin5 (FBN5), was determined with the Arabidopsis thaliana homozygous fbn5-knockout mutant line (SALK_064597) that carries a T-DNA insertion within the FBN5 gene. The fbn5 mutant remained alive, displaying a slow growth and a severe dwarf phenotype. The mutant grown even under growth light conditions at 80 µmol m-2 s-1 showed a drastic decrease in electron transfer activities around PSII, with little change in electron transfer activities around PSI, a phenomenon which was exaggerated under high light stress. The accumulation of plastoquinone-9 (PQ-9) was suppressed in the mutant, and >90% of the PQ-9 pool was reduced under growth light conditions. Non-photochemical quenching (NPQ) in the mutant functioned less efficiently, resulting from little contribution by energy-dependent quenching (qE). The ultrastructure of thylakoids in the mutant revealed that their grana were unstacked and transformed into loose and disordered structures. Light-harvesting complex (LHC)-containing large photosystem complexes and photosystem core complexes in the mutant were less abundant than those in wild-type plants. These results suggest that the lack of FBN5 causes a decrease in PQ-9 and imbalance of the redox state of PQ-9, resulting in misconducting both short-term and long-term control of the input of light energy to photosynthetic reaction centers. Furthermore, in the fbn5 mutant, the expression of genes involved in jasmonic acid biosynthesis was suppressed to ≤10% of that in the wild type under both growth-light and high-light conditions, suggesting that FBN5 functions as a transmitter of 1O2 in the stroma.

A Single Spherical Assembly of Protein Amyloid Fibrils Formed by Laser Trapping.

Protein amyloids have received much attention owing to their correlation with serious diseases and to their promising mechanical and optical properties as future materials. Amyloid formation has been conducted by tuning temperature and chemical conditions, so that its nucleation and the following growth are analyzed as ensemble dynamics. A single spherical assembly of amyloid fibrils of cytochrome c domain-swapped dimer was successfully generated upon laser trapping. The amyloid fibrillar structure was confirmed by fluorescence characterization and electron microscopy. The prepared spheres were further manipulated individually in solution to fabricate a three-dimensional microstructure and a line pattern. Amyloid formation dynamics and amyloid-based microstructure fabrication are demonstrated based on direct observation of a single spherical assembly, which foresees a new approach in amyloid studies.

Domain-swapped dimer of Pseudomonas aeruginosa cytochrome c551: structural insights into domain swapping of cytochrome c family proteins.

Cytochrome c (cyt c) family proteins, such as horse cyt c, Pseudomonas aeruginosa cytochrome c551 (PA cyt c551), and Hydrogenobacter thermophilus cytochrome c552 (HT cyt c552), have been used as model proteins to study the relationship between the protein structure and folding process. We have shown in the past that horse cyt c forms oligomers by domain swapping its C-terminal helix, perturbing the Met-heme coordination significantly compared to the monomer. HT cyt c552 forms dimers by domain swapping the region containing the N-terminal α-helix and heme, where the heme axial His and Met ligands belong to different protomers. Herein, we show that PA cyt c551 also forms domain-swapped dimers by swapping the region containing the N-terminal α-helix and heme. The secondary structures of the M61A mutant of PA cyt c551 were perturbed slightly and its oligomer formation ability decreased compared to that of the wild-type protein, showing that the stability of the protein secondary structures is important for domain swapping. The hinge loop of domain swapping for cyt c family proteins corresponded to the unstable region specified by hydrogen exchange NMR measurements for the monomer, although the swapping region differed among proteins. These results show that the unstable loop region has a tendency to become a hinge loop in domain-swapped proteins.

Maintenance of the secondary structure of horse cytochrome c during the conversion process of monomers to oligomers by addition of ethanol.

We have previously shown that polymerization of cytochrome c (cyt c) occurs by successively domain swapping its C-terminal α-helix in the presence of ethanol. However, the factors that govern the conversion process of monomers to domain-swapped oligomers remain unknown. We found that oligomeric cyt c is produced in the presence of ethanol and the oligomers precipitate due to low solubility. The optical absorption spectra revealed that in the presence of 30-40% ethanol, the Met-heme coordination in cyt c is dissociated. However, according to circular dichroism and small-angle X-ray scattering measurements, the α-helical structure of cyt c is maintained in solution with a little perturbation and the radius of gyration increases slightly but without dissociation of the C-terminal α-helix from the rest of the protein by the addition of ethanol. Solid-state nuclear magnetic resonance spectra showed that oligomeric cyt c in the precipitate also retains most of its α-helical structure. In the transmission electron microscopic image of the precipitate obtained by the addition of ethanol to cyt c, spherical particles with diameters of about 3 nm were detected. These results indicate that oligomeric cyt c forms through a state with the Met80 region locally unfolded, while maintaining the secondary structure, possibly an open monomer.

Retarding activity of 6-O-acyl-D-alloses against plant growth.

The retarding activity of 6-O-dodecanoyl-D-allose against rice growth was higher than that of the octanoate and the decanoate. The activities of 6-O-dodecanoyl-D-glucose, -D-mannose, and -D-galactose against rice seedlings were examined. 6-O-Dodecanoyl-D-allose exhibited the highest activity, suggesting the importance of the alpha-axial hydroxy group at C-3 of D-allose.

Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice.

We collected and completely sequenced 28,469 full-length complementary DNA clones from Oryza sativa L. ssp. japonica cv. Nipponbare. Through homology searches of publicly available sequence data, we assigned tentative protein functions to 21,596 clones (75.86%). Mapping of the cDNA clones to genomic DNA revealed that there are 19,000 to 20,500 transcription units in the rice genome. Protein informatics analysis against the InterPro database revealed the existence of proteins presented in rice but not in Arabidopsis. Sixty-four percent of our cDNAs are homologous to Arabidopsis proteins.