Tohoku University

About: Tohoku University is a education organization based out in Sendai, Japan. It is known for research contribution in the topics: Magnetization & Alloy. The organization has 72116 authors who have published 170791 publications receiving 3941714 citations. The organization is also known as: Tōhoku daigaku.

A Novel Algorithm for Fast and Efficient Speed-Sensorless Maximum Power Point Tracking in Wind Energy Conversion Systems

Abstract: This paper proposes a novel solution to the problems that exist in the conventional hill climb searching (HCS) maximum power point tracking (MPPT) algorithm for the wind energy conversion system. The presented solution not only solves the tracking speed versus control efficiency tradeoff problem of HCS but also makes sure that the changing wind conditions do not lead HCS in the wrong direction. It intelligently adapts the variable step size to keep up with the rapid changes in the wind and seizes the perturbation at the maxima to yield 100% control efficiency. For this purpose, a novel peak detection capability has been devised which, in contrast with conventional peak detection, can work robustly under changing wind conditions. The proposed MPPT performs self-tuning to cope with the nonconstant efficiencies of the generator-converter subsystems-a phenomenon quite rarely discussed in research papers so far. In addition, a smart speed-sensorless scheme has been developed to avoid the use of mechanical sensors. The experimental results confirm that the proposed algorithm is remarkably faster and more efficient than the conventional HCS.

Photosynthesis or persistence: nitrogen allocation in leaves of evergreen and deciduous Quercus species

Abstract: Photosynthetic nitrogen use efficiency (PNUE, photosynthetic capacity per unit leaf nitrogen) is one of the most important factors for the interspecific variation in photosynthetic capacity. PNUE was analysed in two evergreen and two deciduous species of the genus Quercus. PNUE was lower in evergreen than in deciduous species, which was primarily ascribed to a smaller fraction of nitrogen allocated to the photosynthetic apparatus in evergreen species. Leaf nitrogen was further analysed into proteins in the water-soluble, the detergent-soluble, and the detergent-insoluble fractions. It was assumed that the detergent-insoluble protein represented the cell wall proteins. The fraction of nitrogen allocated to the detergent-insoluble protein was greater in evergreen than in deciduous leaves. Thus the smaller allocation of nitrogen to the photosynthetic apparatus in evergreen species was associated with the greater allocation to cell walls. Across species, the fraction of nitrogen in detergent-insoluble proteins was positively correlated with leaf mass per area, whereas that in the photosynthetic proteins was negatively correlated. There may be a trade-off in nitrogen partitioning between components pertaining to productivity (photosynthetic proteins) and those pertaining to persistence (structural proteins). This trade-off may result in the convergence of leaf traits, where species with a longer leaf life-span have a greater leaf mass per area, lower photosynthetic capacity, and lower PNUE regardless of life form, phyllogeny, and biome.

Cloning and characterization of a novel erythroid cell-derived cnc family transcription factor heterodimerizing with the small maf family proteins

Abstract: The chicken beta-globin enhancer is critical for the tissue- and developmental stage-specific expression of the beta-globin genes. This enhancer contains two indispensable cis elements, one containing two GATA sites and the other containing an NF-E2 site. To identify the putative transcription factor acting through the NF-E2 motif in the chicken beta-globin enhancer, we screened chicken cDNA libraries with a mouse p45 NF-E2 cDNA probe and isolated cDNA clones which encode a protein of 582 amino acid residues. This protein contains a region that includes the basic region-leucine zipper domain which is well conserved among members of the CNC family proteins (Cap 'n' collar, p45 NF-E2, LCR-F1, Nrf1, and Nrf2). Hence, we named this protein ECH (erythroid cell-derived protein with CNC homology). ECH is expressed abundantly in cultured erythroid cells undergoing terminal differentiation, peripheral erythrocytes, and some nonhematopoietic tissues. Since most of the cDNA clones obtained from the chicken erythrocyte cDNA library encoded ECH, ECH is likely the predominant CNC family protein present in avian peripheral erythrocytes. Like p45 NF-E2, ECH can heterodimerize with any of the small Maf family proteins and bind the NF-E2 site as a heterodimer in vitro. In a transfection assay, ECH transactivates transcription depending on the presence of NF-E2 sites on the reporter gene plasmid. These results indicate that ECH is likely a key regulator of avian erythropoiesis.