34 research outputs found

    Contenido energético y emisiones de gases de efecto invernadero en el ciclo de vida de un bloque de aulas taller de Arquitectura : Modelo de evaluación y mejoramiento

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    La FAU UNLP posee más de 25 grandes aulas taller construidas desde 1956 a la actualidad. En todos los casos fueron materializadas para ser duraderas, pero sin considerar la variable eficiencia energética en su concepción y materialización. Estas aulas albergan a más de 6000 alumnos y 1000 docentes funcionando de 8:00 a 22:00hs y requieren de constante mantenimiento. En los últimos cuatro años se comenzó un proceso de rehabilitación edilicia y mejora de sus instalaciones. Este trabajo analiza el ciclo de vida de la cuna a la cuna de un bloque de aulas de tres pisos y más de 1000 m2; buscando desarrollar un modelo simplificado de evaluación y mejoramiento térmico y energético que pueda ser contrastado con estándares internacionales. Se presentan los resultados obtenidos a fin de mostrar que es posible plantear aulas de mejor perfomance, minimizando emisiones en su ciclo de vida. Análisis previos muestran que el parque edilicio construido no cumple con estándares mínimos de calidad térmica establecidos en normas nacionales de eficiencia energética edilicia.Facultad de Arquitectura y Urbanism

    Contenido energético y emisiones de gases de efecto invernadero en el ciclo de vida de un bloque de aulas taller de Arquitectura : Modelo de evaluación y mejoramiento

    Get PDF
    La FAU UNLP posee más de 25 grandes aulas taller construidas desde 1956 a la actualidad. En todos los casos fueron materializadas para ser duraderas, pero sin considerar la variable eficiencia energética en su concepción y materialización. Estas aulas albergan a más de 6000 alumnos y 1000 docentes funcionando de 8:00 a 22:00hs y requieren de constante mantenimiento. En los últimos cuatro años se comenzó un proceso de rehabilitación edilicia y mejora de sus instalaciones. Este trabajo analiza el ciclo de vida de la cuna a la cuna de un bloque de aulas de tres pisos y más de 1000 m2; buscando desarrollar un modelo simplificado de evaluación y mejoramiento térmico y energético que pueda ser contrastado con estándares internacionales. Se presentan los resultados obtenidos a fin de mostrar que es posible plantear aulas de mejor perfomance, minimizando emisiones en su ciclo de vida. Análisis previos muestran que el parque edilicio construido no cumple con estándares mínimos de calidad térmica establecidos en normas nacionales de eficiencia energética edilicia.Facultad de Arquitectura y Urbanism

    Sugary interfaces mitigate contact damage where stiff meets soft

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    The byssal threads of the fan shell Atrina pectinata are non-living functional materials intimately associated with living tissue, which provide an intriguing paradigm of bionic interface for robust load-bearing device. An interfacial load-bearing protein (A. pectinata foot protein-1, apfp-1) with L-3,4-dihydroxyphenylalanine (DOPA)-containing and mannose-binding domains has been characterized from Atrina's foot. apfp-1 was localized at the interface between stiff byssus and the soft tissue by immunochemical staining and confocal Raman imaging, implying that apfp-1 is an interfacial linker between the byssus and soft tissue, that is, the DOPA-containing domain interacts with itself and other byssal proteins via Fe3(+)-DOPA complexes, and the mannose-binding domain interacts with the soft tissue and cell membranes. Both DOPA-and sugar-mediated bindings are reversible and robust under wet conditions. This work shows the combination of DOPA and sugar chemistry at asymmetric interfaces is unprecedented and highly relevant to bionic interface design for tissue engineering and bionic devices

    Understanding Marine Mussel Adhesion

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    In addition to identifying the proteins that have a role in underwater adhesion by marine mussels, research efforts have focused on identifying the genes responsible for the adhesive proteins, environmental factors that may influence protein production, and strategies for producing natural adhesives similar to the native mussel adhesive proteins. The production-scale availability of recombinant mussel adhesive proteins will enable researchers to formulate adhesives that are water-impervious and ecologically safe and can bind materials ranging from glass, plastics, metals, and wood to materials, such as bone or teeth, biological organisms, and other chemicals or molecules. Unfortunately, as of yet scientists have been unable to duplicate the processes that marine mussels use to create adhesive structures. This study provides a background on adhesive proteins identified in the blue mussel, Mytilus edulis, and introduces our research interests and discusses the future for continued research related to mussel adhesion

    Oxidative protein labeling in mass-spectrometry-based proteomics

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    Oxidation of proteins and peptides is a common phenomenon, and can be employed as a labeling technique for mass-spectrometry-based proteomics. Nonspecific oxidative labeling methods can modify almost any amino acid residue in a protein or only surface-exposed regions. Specific agents may label reactive functional groups in amino acids, primarily cysteine, methionine, tyrosine, and tryptophan. Nonspecific radical intermediates (reactive oxygen, nitrogen, or halogen species) can be produced by chemical, photochemical, electrochemical, or enzymatic methods. More targeted oxidation can be achieved by chemical reagents but also by direct electrochemical oxidation, which opens the way to instrumental labeling methods. Oxidative labeling of amino acids in the context of liquid chromatography(LC)–mass spectrometry (MS) based proteomics allows for differential LC separation, improved MS ionization, and label-specific fragmentation and detection. Oxidation of proteins can create new reactive groups which are useful for secondary, more conventional derivatization reactions with, e.g., fluorescent labels. This review summarizes reactions of oxidizing agents with peptides and proteins, the corresponding methodologies and instrumentation, and the major, innovative applications of oxidative protein labeling described in selected literature from the last decade

    Structural Features Underlying the Multisite Phosphorylation of the A Domain of the NF-AT4 Transcription Factor by Protein Kinase CK1\u2020

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    The phosphorylation and dephosphorylation of the NF-AT family of transcription factors play a key role in the activation of T lymphocytes and in the control of the immune response. The mechanistic aspects of NF-AT4 phosphorylation by protein kinase CK1 have been studied in this work with the aid of a series of 27 peptides, reproducing with suitable modifications the regions of NF-AT4 that have been reported to be phosphorylated by this protein kinase. The largest parent peptide, representing the three regions A, Z, and L spanning amino acids 173-218, is readily phosphorylated by CK1 at seryl residues belonging to the A2 segment, none of which fulfill the canonical consensus sequence for CK1. An acidic cluster of amino acids in the linker region between domains A and Z is essential for high-efficiency phosphorylation of the A2 domain, as shown by the increase in K(m) caused by a deletion of the linker region or a substitution of the acidic residues with glycines. Individual substitutions with alanine of each of the five serines in the A2 domain (S-177, S-180, S-181, S-184, and S-186) reduce the phosphorylation rate, the most detrimental effect being caused by Ser177 substitution which results in a 10-fold drop in V(max). On the contrary, the replacement of Ser177 with phosphoserine triggers a hierarchical effect with a dramatic improvement in phosphorylation efficiency, which no longer depends on the linker region for optimal efficiency. These data are consistent with a two-phase phosphorylation mechanism of NF-AT4 by CK1, initiated by the linker region which provides a functional docking site for CK1 and allows the unorthodox phosphorylation of Ser177; once achieved, this phosphoserine residue primes the phosphorylation of other downstream seryl residues, according to a hierarchical mechanism typically exploited by CK1
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