Acid-mediated topological control in a functionalized foldamer

Induced conformational change provides a powerful mechanism to modulate the structure and function of molecules. Here we describe the synthesis of chiral, surface-functionalized oligomeric pyridine/imidazolidin-2-one foldamers, and interrogate their acid-mediated transition between linear and helical topologies.

Fabrication and evaluation of NiO/Y2O3-stabilized-ZrO2 hollow fibers for anode-supported micro-tubular solid oxide fuel cells

In this work NiO/3mol% Y₂O₃-ZrO₂ (3YSZ) and NiO/8mol% Y₂O₃-ZrO₂ (8YSZ) hollow fibers were prepared by phase-inversion. The effect of different kinds of YSZ (3YSZ and 8YSZ) on the porosity, electrical conductivity, shrinkage and flexural strength of the hollow fibers were systematically evaluated. When compared with Ni-8YSZ the porosity and shrinkage of Ni-3YSZ hollow fibers increases while the electrical conductivity decreases, while at the same time also exhibiting enhanced flexural strength. Single cells with Ni-3YSZ and Ni-8YSZ hollow fibers as the supported anode were successfully fabricated showing maximum power densities of 0.53 and 0.67Wcm^-2 at 800°C, respectively. Furthermore, in order to improve the cell performance, a Ni-8YSZ anode functional layer was added between the electrolyte and Ni-YSZ hollow fiber. Here enhanced peak power densities of 0.79 and 0.73Wcm^-2 were achieved at 800°C for single cells with Ni-3YSZ and Ni-8YSZ hollow fibers, respectively.

Preparation and characterization of Pr0.6Sr0.4FeO3-δ-Ce0.9Pr0.1O2-δ nanofiber structured composite cathode for IT-SOFCs

In this work, Pr_0.6Sr_0.4FeO_3-δ -Ce_0.9Pr_0.1O_2-δ (PSFO-CPO) nanofibers were synthesized by a one-step electrospin technique for use in intermediate-temperature solid oxide fuel cell (IT-SOFC) applications. PSFO-CPO nanofibers were produced with a diameter of about 100nm and lengths exceeding tens of microns. The thermal expansion coefficient (TEC) matches with standard GDC electrolytes and the resulting conductivity also satisfies the needs of IT-SOFCs cathodes. EIS analysis of the nanofiber structured electrode gives a polarization resistance of 0.072Ωcm² at 800°C, smaller than that from the powdered cathode with the same composition. The excellent electrochemical performance can be attributed to the well-constructed microstructure of the nanofiber structured cathode, which promotes surface oxygen diffusion and charge transfer processes. All the results imply that the one-step electrospin method is a facile and practical way of improving the cathode properties and that PSFO-CPO is a promising cathode material for IT-SOFCs.

Fabrication and characterization of SSZ tape cast electrolyte-supported solid oxide fuel cells

A 10 mol%Sc₂O₃, 1 mol%CeO₂ stabilized-ZrO₂ (SSZ) powder was successfully prepared using the sol-gel method. Subsequent SSZ electrolyte pellets were prepared by tape casting technique and sintered at 1400 °C, 1450 °C, 1500 °C, 1550 °C and 1600 °C. These were characterized by X-ray diffraction (XRD), scanning electron microscopy (SEM) and electrochemical impedance spectroscopy (EIS). SSZ showed a pure cubic phase after sintering, the grain size of SSZ increased with the increase of sintering temperature. The SSZ sintered at 1550 °C showed the highest ion conductivity. The maximum power densities of Ni-SSZ/SSZ/La_0.8Sr_0.2MnO_3-δ (LSM)-SSZ single cells sintered at 1550 °C were 0.18, 0.36, 0.51 and 0.72 W cm^-2 at 650, 700, 750 and 800 °C, respectively. The polarization resistance (R_p) of the single cell attained 0.201 Ω cm² at 800 °C.

Sellar Spine Associated with Endocrine and Neuro-Ophthalmological Manifestations

A case of sellar spine, associated with neuro-ophthalmological and endocrine abnormalities, is reported. The case described is a rare malformation, of which the authors found only six cases in the literature.

Impacto hidrológico de distintas estrategias agrícolas en el Chaco semiárido

En las últimas décadas, el Chaco semiárido sudamericano ha sido intensamente deforestado para producir cultivos agrícolas y pasturas. En planicies semiáridas de muy escaso relieve, el reemplazo de la vegetación perenne nativa por cultivos anuales, de menor capacidad evapotranspirativa, puede alterar el balance hidrológico generando pulsos de drenaje profundo, originalmente inexistentes, que pueden desencadenar procesos de recarga, ascenso freático y salinización secundaria. A su vez, la magnitud y frecuencia de los eventos de drenaje dependen de las prácticas de manejo agrícola empleadas por los productores. Las prácticas que hacen un uso más exhaustivo del agua disponible contribuirían a reducir el drenaje y el riesgo de salinización, pero representan un mayor riesgo productivo en años secos. Por otro lado, las prácticas más conservativas tienden a estabilizar la producción con esquemas de menores requerimientos hídricos pero son más propensas a generar drenaje, especialmente en años húmedos. El objetivo de esta tesis fue entender el impacto hidrológico de la agricultura en el Chaco semiárido y analizar la posibilidad de manejar la hidrología de los agroecosistemas para conciliar objetivos productivos y ambientales. Mediciones de campo en Bandera, uno de los principales polos agrícolas de la región, permitieron constatar una situación de alto riesgo de salinización secundaria determinado por altos niveles de salinidad del suelo, napas salinas cercanas a la superficie y procesos de recarga freática en lotes agrícolas, no detectados en los escasos relictos de bosque nativo. Análisis biofísicos con sensores remotos e información provista por productores locales, permitieron identificar los principales esquemas de cultivo empleados y estimar el riesgo productivo y el drenaje generado en cada uno de ellos ante situaciones de diferente oferta hídrica. Finalmente, un balance hídrico regional permitió detectar las zonas más vulnerables de la región y evaluar los beneficios productivos e hidrológicos de alternar manejos conservativos o intensivos según la oferta hídrica esperada.

El problema de Metapán

Cada río erosiona hacia abajo en su cauce superior,mientras en su cauce inferior tiene lugar la acumulación de los materiales transportados en su propio lecho. El transporte del material es una función de la velocidad que tiene las aguas del río.Cada río trata de establecer un desnivel continuo desde su nacimiento hasta la base de erosión nivelando saltos y otras interrupciones bruscas de su lecho el límite de su cauce inferior es decir zona de acumulación y cause superior es decir zona de erosión,camina durante este proceso hacia arriba.Dicho límite,en el río San José, se encuentra actualmente a unos 2,5 Km río arriba de Metapán.Desde aquí hasta la embocadura,el lecho del río se levanta continuamente por la acumulación de los sedimentos. Si se pudiera bajar el nivel de la laguna de Metapán el río San José estaría forzado a ajustar el desnivel de su lecho conforme al nuevo nivel del lago,es decir el río erosionaría de nuevo una parte de los sedimentos depositados por el mismo bajando su lecho hasta encontrar su nuevo equilibrio.

Revistas semanales del tiempo de San Salvador desde el 1 de enero hasta el 29 de junio de 1952

El departamento de meteorología del Instituto Tropical de Investigaciones Científicas elabora semanalmente informes meteorológicos que comprenden las alturas de lluvias y las temperaturas extremas diarias tomando como base las respectivas observaciones del observatorio nacional (OBS NAC)y del Instituto Tropical (ITIC). El observatorio nacional esta situado en la ciudad, calle Arce No 142B, mientras que el Instituto Tropical esta ubicado fuera del limite urbano al noroeste y a 2,5 km de distancia del observatorio Nacional. El Instituto Tropical también publica en su "boletín Meteorológico de San Salvador. El boletín contiene ademas gráficas acerca de la presión atmosférica, de la oscilación diaria de la temperatura, dirección y fuerza del viento y temperatura del suelo.

Global citizenship: an education or an identity?

This paper considers the recent focus on citizenship within education by taking curricular reform within Scottish secondary schooling and its linkage with higher education as a case study. In Scotland the Curriculum for Excellence reform places citizenship as one of four main capacities that pupils must work towards as part of their education. Likewise, there has been a move in within the Scottish higher education Enhancement Themes framework to include citizenship as part of graduate attributes that students work towards as they progress through their courses. A unifying theme in these reforms is the need for students to take a global perspective and work across different disciplines by, for example, considering how knowledge relates to wider issues such as in relation to sustainable development, e-democracy or human rights. One feature that unites these disparate areas is that, above all, students must learn to be active through the acquisition of appropriate knowledge and skills. In this model of citizenship education, learners are enabled to develop their sense of citizenship identity in response to a fast-paced world of innovation and change. Citizenship is therefore linked to a futurist agenda, where the learner-citizen is positioned as an ongoing project, as something to be worked at or perhaps worked on. However, this kind of notion of agency is an expression of an ideological construction of the citizen as a flexible resource for society. Such citizens are active in the sense of being adaptive to change through utilizing intellectual skills but without a sense of identity grounded in one’s commitments or reflexive engagement with different forms of understanding. The paper offers a critical assessment of this learner-citizen discourse as focusing on ratiocination rather than relational identity.

Microfluidic platforms for the characterization of in meso membrane protein crystallization

Membrane proteins, which reside in the membranes of cells, play a critical role in many important biological processes including cellular signaling, immune response, and material and energy transduction. Because of their key role in maintaining the environment within cells and facilitating intercellular interactions, understanding the function of these proteins is of tremendous medical and biochemical significance. Indeed, the malfunction of membrane proteins has been linked to numerous diseases including diabetes, cirrhosis of the liver, cystic fibrosis, cancer, Alzheimer's disease, hypertension, epilepsy, cataracts, tubulopathy, leukodystrophy, Leigh syndrome, anemia, sensorineural deafness, and hypertrophic cardiomyopathy.1-3 However, the structure of many of these proteins and the changes in their structure that lead to disease-related malfunctions are not well understood. Additionally, at least 60% of the pharmaceuticals currently available are thought to target membrane proteins, despite the fact that their exact mode of operation is not known.4-6 Developing a detailed understanding of the function of a protein is achieved by coupling biochemical experiments with knowledge of the structure of the protein. Currently the most common method for obtaining three-dimensional structure information is X-ray crystallography. However, no a priori methods are currently available to predict crystallization conditions for a given protein.7-14 This limitation is currently overcome by screening a large number of possible combinations of precipitants, buffer, salt, and pH conditions to identify conditions that are conducive to crystal nucleation and growth.7,9,11,15-24 Unfortunately, these screening efforts are often limited by difficulties associated with quantity and purity of available protein samples. While the two most significant bottlenecks for protein structure determination in general are the (i) obtaining sufficient quantities of high quality protein samples and (ii) growing high quality protein crystals that are suitable for X-ray structure determination,7,20,21,23,25-47 membrane proteins present additional challenges. For crystallization it is necessary to extract the membrane proteins from the cellular membrane. However, this process often leads to denaturation. In fact, membrane proteins have proven to be so difficult to crystallize that of the more than 66,000 structures deposited in the Protein Data Bank,48 less than 1% are for membrane proteins, with even fewer present at high resolution (< 2Å)4,6,49 and only a handful are human membrane proteins.49 A variety of strategies including detergent solubilization50-53 and the use of artificial membrane-like environments have been developed to circumvent this challenge.43,53-55 In recent years, the use of a lipidic mesophase as a medium for crystallizing membrane proteins has been demonstrated to increase success for a wide range of membrane proteins, including human receptor proteins.54,56-62 This in meso method for membrane protein crystallization, however, is still by no means routine due to challenges related to sample preparation at sub-microliter volumes and to crystal harvesting and X-ray data collection. This dissertation presents various aspects of the development of a microfluidic platform to enable high throughput in meso membrane protein crystallization at a level beyond the capabilities of current technologies. Microfluidic platforms for protein crystallization and other lab-on-a-chip applications have been well demonstrated.9,63-66 These integrated chips provide fine control over transport phenomena and the ability to perform high throughput analyses via highly integrated fluid networks. However, the development of microfluidic platforms for in meso protein crystallization required the development of strategies to cope with extremely viscous and non-Newtonian fluids. A theoretical treatment of highly viscous fluids in microfluidic devices is presented in Chapter 3, followed by the application of these strategies for the development of a microfluidic mixer capable of preparing a mesophase sample for in meso crystallization at a scale of less than 20 nL in Chapter 4. This approach was validated with the successful on chip in meso crystallization of the membrane protein bacteriorhodopsin. In summary, this is the first report of a microfluidic platform capable of performing in meso crystallization on-chip, representing a 1000x reduction in the scale at which mesophase trials can be prepared. Once protein crystals have formed, they are typically harvested from the droplet they were grown in and mounted for crystallographic analysis. Despite the high throughput automation present in nearly all other aspects of protein structure determination, the harvesting and mounting of crystals is still largely a manual process. Furthermore, during mounting the fragile protein crystals can potentially be damaged, both from physical and environmental shock. To circumvent these challenges an X-ray transparent microfluidic device architecture was developed to couple the benefits of scale, integration, and precise fluid control with the ability to perform in situ X-ray analysis (Chapter 5). This approach was validated successfully by crystallization and subsequent on-chip analysis of the soluble proteins lysozyme, thaumatin, and ribonuclease A and will be extended to microfluidic platforms for in meso membrane protein crystallization. The ability to perform in situ X-ray analysis was shown to provide extremely high quality diffraction data, in part as a result of not being affected by damage due to physical handling of the crystals. As part of the work described in this thesis, a variety of data collection strategies for in situ data analysis were also tested, including merging of small slices of data from a large number of crystals grown on a single chip, to allow for diffraction analysis at biologically relevant temperatures. While such strategies have been applied previously,57,59,61,67 they are potentially challenging when applied via traditional methods due to the need to grow and then mount a large number of crystals with minimal crystal-to-crystal variability. The integrated nature of microfluidic platforms easily enables the generation of a large number of reproducible crystallization trials. This, coupled with in situ analysis capabilities has the potential of being able to acquire high resolution structural data of proteins at biologically relevant conditions for which only small crystals, or crystals which are adversely affected by standard cryocooling techniques, could be obtained (Chapters 5 and 6). While the main focus of protein crystallography is to obtain three-dimensional protein structures, the results of typical experiments provide only a static picture of the protein. The use of polychromatic or Laue X-ray diffraction methods enables the collection of time resolved structural information. These experiments are very sensitive to crystal quality, however, and often suffer from severe radiation damage due to the intense polychromatic X-ray beams. Here, as before, the ability to perform in situ X-ray analysis on many small protein crystals within a microfluidic crystallization platform has the potential to overcome these challenges. An automated method for collecting a "single-shot" of data from a large number of crystals was developed in collaboration with the BioCARS team at the Advanced Photon Source at Argonne National Laboratory (Chapter 6). The work described in this thesis shows that, even more so than for traditional structure determination efforts, the ability to grow and analyze a large number of high quality crystals is critical to enable time resolved structural studies of novel proteins. In addition to enabling X-ray crystallography experiments, the development of X-ray transparent microfluidic platforms also has tremendous potential to answer other scientific questions, such as unraveling the mechanism of in meso crystallization. For instance, the lipidic mesophases utilized during in meso membrane protein crystallization can be characterized by small angle X-ray diffraction analysis. Coupling in situ analysis with microfluidic platforms capable of preparing these difficult mesophase samples at very small volumes has tremendous potential to enable the high throughput analysis of these systems on a scale that is not reasonably achievable using conventional sample preparation strategies (Chapter 7). In collaboration with the LS-CAT team at the Advanced Photon Source, an experimental station for small angle X-ray analysis coupled with the high quality visualization capabilities needed to target specific microfluidic samples on a highly integrated chip is under development. Characterizing the phase behavior of these mesophase systems and the effects of various additives present in crystallization trials is key for developing an understanding of how in meso crystallization occurs. A long term goal of these studies is to enable the rational design of in meso crystallization experiments so as to avoid or limit the need for high throughput screening efforts. In summary, this thesis describes the development of microfluidic platforms for protein crystallization with in situ analysis capabilities. Coupling the ability to perform in situ analysis with the small scale, fine control, and the high throughput nature of microfluidic platforms has tremendous potential to enable a new generation of crystallographic studies and facilitate the structure determination of important biological targets. The development of platforms for in meso membrane protein crystallization is particularly significant because they enable the preparation of highly viscous mixtures at a previously unachievable scale. Work in these areas is ongoing and has tremendous potential to improve not only current the methods of protein crystallization and crystallography, but also to enhance our knowledge of the structure and function of proteins which could have a significant scientific and medical impact on society as a whole. The microfluidic technology described in this thesis has the potential to significantly advance our understanding of the structure and function of membrane proteins, thereby aiding the elucidation of human biology, the development of pharmaceuticals with fewer side effects for a wide range of diseases. References (1) Quick, M.; Javitch, J. A. P Natl Acad Sci USA 2007, 104, 3603. (2) Trubetskoy, V. S.; Burke, T. J. Am Lab 2005, 37, 19. (3) Pecina, P.; Houstkova, H.; Hansikova, H.; Zeman, J.; Houstek, J. Physiol Res 2004, 53, S213. (4) Arinaminpathy, Y.; Khurana, E.; Engelman, D. M.; Gerstein, M. B. Drug Discovery Today 2009, 14, 1130. (5) Overington, J. P.; Al-Lazikani, B.; Hopkins, A. L. Nat Rev Drug Discov 2006, 5, 993. (6) Dauter, Z.; Lamzin, V. S.; Wilson, K. S. Current Opinion in Structural Biology 1997, 7, 681. (7) Hansen, C.; Quake, S. R. Current Opinion in Structural Biology 2003, 13, 538. (8) Govada, L.; Carpenter, L.; da Fonseca, P. C. A.; Helliwell, J. 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Estudio de la salinidad en la cuenca baja El Guayabo, en los municipios de Tecoluca y Zacatecoluca

La presente investigación hidrogeológica se realizó en la planicie costera de la cuenca El Guayabo, y está orientada a determinar el fenómeno de la salinidad del acuífero. La cuenca El Guayabo se ubica en los municipios de Zacatecoluca y Tecoluca y forma parte de la Región hidrográfica Jiboa, dentro de la Zona Prioritaria Estero de Jaltepeque. La zona está compuesta por la unidad de acuífero poroso de gran extensión, predominando capas de sedimentos fluviales, donde parámetros físico químicos del agua subterránea reflejan la incidencia de la intrusión marina en áreas próximas a la costa, la cual ha sido definida mediante la distribución de ion Cloruro, conductividad eléctrica y valores de las relaciones iónicas, así como se ha observado, tierra adentro, niveles de salinidad alta que se originan por otras causas, siendo las actividades antrópicas propias de la zona la probable causa de este deterioro que en la época de lluvias se observó incrementado. Los resultados que se presentan servirán de línea base de la caracterización hidroquímica del agua en el acuífero costero de la cuenca El Guayabo, que podrá servir para su monitoreo y seguimiento, principalmente en las zonas con mayor grado de vulnerabilidad