994 resultados para Guy anchors
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Fil: Astarita, Carlos Alberto Tomás. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.
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En este trabajo se plantea un proceso de investigación sobre la arquitectura con cartón, que va desde el estudio del material y la arquitectura construida, hasta la profundización en las ideas del arquitecto Guy Rottier sobre estas arquitecturas, plasmadas en su totalidad en el proyecto de la village en carton. El trabajo se ha desarrollado en 5 fases: En la primera fase se pretende demostrar el interés del cartón como material para la arquitectura y las nuevas posibilidades que abre su uso. En la segunda fase se estudia el cartón desde un punto de vista técnico, investigando sobre los distintos productos que ofrece el mercado y sus características técnicas. La tercera fase consiste en una investigación de la obra construida utilizando el cartón como material principal. Se han elegido una serie de obras representativas debido al tipo de cartón que utilizan y el sistema constructivo, clasificadas en función de su escala. En la cuarta fase se expone la vida, obra e ideas sobre la arquitectura de Guy Rottier, arquitecto de la village en carton. Rottier es un adelantado a su tiempo, ya en los años 60 plantea en sus proyectos temas tan actuales como la arquitectura sostenible, la arquitectura efímera o el aprovechamiento de la energía solar. La quinta y última fase consiste en el desarrollo del proyecto de la village en carton de Guy Rottier, utilizando todo el conocimiento adquirido en las anteriores fases del trabajo. En el desarrollo del proyecto se especifican aspectos como la propuesta de diseño, los tipos de cartón apropiados para cada elemento, el sistema de montaje y una definición completa del mismo a nivel constructivo.
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https://bluetigercommons.lincolnu.edu/lgaines_sec1/1021/thumbnail.jpg
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Bibliografia.
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Inclui bibliografia.
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Facile modification of oligodeoxyribonucleotides is required for efficient immobilization to a pre-activated glass surface. This report presents an oligodeoxyribonucleotide which contains a hairpin stem–loop structure with multiple phosphorothioate moieties in the loop. These moieties are used to anchor the oligo to glass slides that are pre-activated with bromoacetamidopropylsilane. The efficiency of the attachment reaction was improved by increasing the number of phosphorothioates in the loop, as shown in the remarkable enhancement of template hybridization and single base extension through catalysis by DNA polymerase. The loop and stem presumably serve as lateral spacers between neighboring oligodeoxyribonucleotides and as a linker arm between the glass surface and the single-stranded sequence of interest. The oligodeoxyribonucleotides of this hairpin stem–loop architecture with multiple phosphorothioate moieties have broad application in DNA chip-based gene analysis.
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Surface proteins of Gram-positive bacteria play important roles during the pathogenesis of human infections and require sortase for anchoring to the cell-wall envelope. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine (T) and the amino group of cell-wall crossbridges. The NMR structure of sortase reveals a unique β-barrel structure, in which the active-site sulfhydryl of cysteine-184 is poised for ionization by histidine-120, presumably enabling the resultant thiolate to attack the LPXTG peptide. Calcium binding near the active site stimulates catalysis, possibly by altering the conformation of a surface loop that recognizes newly translocated polypeptides. The structure suggests a mechanistic relationship to the papain/cathepsin proteases and should facilitate the design of new antiinfective agents.
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The search for novel leads is a critical step in the drug discovery process. Computational approaches to identify new lead molecules have focused on discovering complete ligands by evaluating the binding affinity of a large number of candidates, a task of considerable complexity. A new computational method is introduced in this work based on the premise that the primary molecular recognition event in the protein binding site may be accomplished by small core fragments that serve as molecular anchors, providing a structurally stable platform that can be subsequently tailored into complete ligands. To fulfill its role, we show that an effective molecular anchor must meet both the thermodynamic requirement of relative energetic stability of a single binding mode and its consistent kinetic accessibility, which may be measured by the structural consensus of multiple docking simulations. From a large number of candidates, this technique is able to identify known core fragments responsible for primary recognition by the FK506 binding protein (FKBP-12), along with a diverse repertoire of novel molecular cores. By contrast, absolute energetic criteria for selecting molecular anchors are found to be promiscuous. A relationship between a minimum frustration principle of binding energy landscapes and receptor-specific molecular anchors in their role as "recognition nuclei" is established, thereby unraveling a mechanism of lead discovery and providing a practical route to receptor-biased computational combinatorial chemistry.
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Contains medical cases copied by James Lloyd (1728-1810), primarily between 1751 and 1754, from Mr. Steed, an apothecary at Guy's Hospital in London, England. The volume has additional medical cases dating from 1780 to 1787. Lloyd transcribed the names, ages, and symptoms of the patients, as well as the medicines and medical care delivered to them. The volume is divided into chapters based on the type of case, which included vision loss; fluor albus, or leucorrhoea; diabetes; and dysentery. There is also a letter pasted into the volume addressed to Dr. Brigham of the Boston Medical Library Association from Lloyd's great-grandson, dated 4 November 1887.