7 research outputs found

    Influence of resource definition on defining a WEC optimal size

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    International audienceThis work is a follow up from two previous studies which have been investigating the difference in wave resource between sites and the impact this has on the optimal Wave Energy Converter (WEC) size using scatter diagrams of the sites only. This study expands these works by using omni-directional spectra time series to describe the wave resource instead of scatter diagrams. Two well known wave energy test sites are considered: EMEC (Billia Crew) in the North of Scotland and the SEM-REV on the West coast of France. The sloped IPS buoy is used as a case study, and a succinct description is provided. As in previous work, only the hydrodynamic power capture is considered, and no power-takeoff efficiency or cap are introduced. For both sites, around one full year of data is available. Using both the scatter diagrams and the spectra directly, WEC performance metrics are computed for each site and compared. The results show that using spectral time series instead of the scatter diagrams yield lower annual energy productions, and that the highest average capture width ratio is obtained for larger scale devices. Spectral time series allows also the establishment of a simple O&M model. The effect on device availability of annual planned downtime days, of annual failure rates of 1, 3 and 5 and of operability threshold of 2m and 2.5m are investigated. The results show that larger scales might indeed have higher availability, but are exposed to higher risks

    The polyomavirus BK agnoprotein co-localizes with lipid droplets

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    Agnoprotein encoded by human polyomavirus BK (BKV) is a late cytoplasmic protein of 66 amino acids (aa) of unknown function. Immunofluorescence microscopy revealed a fine granular and a vesicular distribution in donut-like structures. Using BKV(Dunlop)-infected or agnoprotein-transfected cells, we investigated agnoprotein co-localization with subcellular structures. We found that agnoprotein co-localizes with lipid droplets (LD) in primary human renal tubular epithelial cells as well as in other cells supporting BKV replication in vitro (UTA, Vero cells). Using agnoprotein-enhanced green fluorescent protein (EGFP) fusion constructs, we demonstrate that agnoprotein aa 20-42 are required for targeting LD, whereas aa 1-20 or aa 42-66 were not. Agnoprotein aa 22-40 are predicted to form an amphipathic helix, and mutations A25D and F39E, disrupting its hydrophobic domain, prevented LD targeting. However, changing the phosphorylation site serine-11 to alanine or aspartic acid did not alter LD co-localization. Our findings provide new clues to unravel agnoprotein function

    Glia–neuron interactions in neurological diseases: Testing non-cell autonomy in a dish

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