New On-Line Excitation-System Ground Fault Location Method Tested in a 106 MVA Synchronous Generator

In this paper, a novel excitation-system ground-fault location method is described and tested in a 106 MVA synchronous machine. In this unit, numerous rotor ground-fault trips took place always about an hour after the synchronization to the network. However, when the field winding insulation was checked after the trips, there was no failure. The data indicated that the faults in the rotor were caused by centrifugal forces and temperature. Unexpectedly, by applying this new method, the failure was located in a cable between the excitation transformer and the automatic voltage regulator. In addition, several intentional ground faults were performed along the field winding with different fault resistance values, in order to test the accuracy of this method to locate defects in rotor windings of large generators. Therefore, this new on-line rotor ground-fault detection algorithm is tested in high-power synchronous generators with satisfactory results.

Plan de ordenación de los pastos en la dehesa Lomo Peral, monte de utilidad pública número 106 en Prádena del Rincón (Madrid)

Este trabajo pretende ser la base para la implantación de un Plan de Ordenación de los pastos de la dehesa Lomo Peral, Monte de Utilidad Pública número 106, que se encuentra en el municipio Prádena del Rincón, en la Comunidad de Madrid (CM). A partir de las Instrucciones de Ordenación de Montes de la Comunidad de Madrid (2010), se ha elaborado un análisis de la situación agroforestal actual de la dehesa, su potencial para producir pastos y las posibles salidas al mercado de los productos derivados de su explotación, en este caso ganadería ovina y bovina.

La Traca : semanari pa la gent de tro: Año IV Número 106 - 1 enero 1887

Recurso electrónico. Valencia: BVNP, 2014

Recombinant scrapie-like prion protein of 106 amino acids is soluble

The N terminus of the scrapie isoform of prion protein (PrPSc) can be truncated without loss of scrapie infectivity and, correspondingly, the truncation of the N terminus of the cellular isoform, PrPC, still permits conversion into PrPSc. To assess whether additional segments of the PrP molecule can be deleted, we previously removed regions of putative secondary structure in PrPC; in the present study we found that deletion of each of the four predicted helices prevented PrPSc formation, as did deletion of the stop transfer effector region and the C178A mutation. Removal of a 36-residue loop between helices 2 and 3 did not prevent formation of protease-resistant PrP; the resulting scrapie-like protein, designated PrPSc106, contained 106 residues after cleavage of an N-terminal signal peptide and a C-terminal sequence for glycolipid anchor addition. Addition of the detergent Sarkosyl to cell lysates solubilized PrPSc106, which retained resistance to digestion by proteinase K. These results suggest that all the regions of proposed secondary structure in PrP are required for PrPSc formation, as is the disulfide bond stabilizing helices 3 and 4. The discovery of PrPSc106 should facilitate structural studies of PrPSc, investigations of the mechanism of PrPSc formation, and the production of PrPSc-specific antibodies.