New System for the Acceleration of the Airflow in Wind Turbines

Background: This patent is based on the wind industry technology called Diffuser Augmented Wind Turbines (DAWTs). This technology consists of a horizontal axis wind turbine, which is housed inside a duct with diverging section in the direction of the free air stream. In this paper, a review of preceding patents related to this technology is carried out. Objective: This paper presents an innovative patent to improve the performance of horizontal axis wind turbines. In particular, this system is aimed at improving the performance of those turbines that otherwise might not be installed due to the low wind resource existing at certain locations. Methods: The most innovative elements of this patent are: (1) the semi-spherical grooves, which are mechanized on the surface of the two diffusers in order to guarantee a more energetic boundary layer; (2) the coaxial diffuser, which is located downwind following the first diffuser in order to increase the suction effect on the air mass close to the inlet; (3) the coaxial rings located around the first diffuser outlet, which are used to deflect the external airflow toward the turbine wake; and (4), the selforientating system to orientate the system by the prevailing wind direction. Results: An application of the patent for increasing the power generated by a horizontal axis wind turbine with three blades is presented. The patent is designed and its performance is evaluated by using a Computational Fluid Dynamics code. The numerical results show that this system rises the airflow going through the rotor of the turbine. Conclusion: The patented device is an original contribution aimed at enabling a more profitable installation of wind turbines in places where the wind resource is insufficient because of the wind shear caused both by the proximity of the earth and the obstacles on the earth surface.This work was supported by the OASIS Research Project that was cofinanced by CDTI (Spanish Science and Innovation Ministry) and developed with the Spanish companies: Iridium, OHL Concesiones, Abertis, Sice, Indra, Dragados, OHL, Geocisa, GMV, Asfaltos Augusta, Hidrofersa, Eipsa, PyG, CPS, AEC and Torre de Comares Arquitectos S.L and 16 research centres. The authors also acknowledge the partial funding with FEDER funds under the Research Project FC-15-GRUPIN14-004. Finally, we also thank Swanson Analysis Inc. for the use of ANSYS University Research programs as well as the Workbench simulation environment

Rapid and sensitive identification of major histocompatibility complex class I-associated tumor peptides by Nano-LC MALDI MS/MS

Identification of major histocompatibility complex (MHC)-associated peptides recognized by T-lymphocytes is a crucial prerequisite for the detection and manipulation of specific immune responses in cancer, viral infections, and autoimmune diseases. Unfortunately immunogenic peptides are less abundant species present in highly complex mixtures of MHC-extracted material. Most peptide identification strategies use microcapillary LC coupled to nano-ESI MS/MS in a challenging on-line approach. Alternatively MALDI PSD analysis has been applied for this purpose. We report here on the first off-line combination of nanoscale (nano) LC and MALDI TOF/TOF MS/MS for the identification of naturally processed MHC peptide ligands. These peptides were acid-eluted from human leukocyte antigen (HLA)-A2, HLA-A3, and HLA-B/-C complexes separately isolated from a renal cell carcinoma cell lysate using HLA allele-specific antibodies. After reversed-phase HPLC, peptides were further fractionated via nano-LC. This additional separation step provided a substantial increase in the number of detectable candidate species within the complex peptide pools. MALDI MS/MS analysis on nano-LC-separated material was then sufficiently sensitive to rapidly identify more than 30 novel HLA-presented peptide ligands. Peptide sequences contained perfect anchor amino acid residues described previously for HLA-A2, HLA-A3, and HLA-B7. The most promising candidate for a T-cell epitope is an HLA-B7-binding nonamer peptide derived from the tumor-associated gene NY-BR-16. To demonstrate the sensitivity of our approach we characterized peptides binding to HLA-C molecules that are usually expressed at the cell surface at approximately only 10% the levels of HLA-A or HLA-B. In fact, multiple renal cell carcinoma peptides were identified that contained anchor amino acid residues of HLA-Cw5 and HLA-Cw7. We conclude that the nano-LC MALDI MS/MS approach is a sensitive tool for the rapid and automated identification of MHC-associated tumor peptides.Sandra Hofmann, Matthias Glückmann, Sandra Kausche, Andrea Schmidt, Carsten Corvey, Rudolf Lichtenfels, Christoph Huber, Christian Albrecht, Michael Karas and Wolfgang Her