2 resultados para PAT assay

em AMS Tesi di Laurea - Alm@DL - Università di Bologna


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This dissertation deals with the translations of seven books for children written by the Chicano author Pat Mora. I started to be interested in the Chicano world, a world suspended between Mexico and the United States, after reading a book by Sandra Cisneros. I decided to deepen my curiosity and for this reason, I discovered a hybrid reality full of history, culture and traditions. In this context, the language used is characterized by a continuous code switching between Spanish and English and I thought it was an interesting phenomenon from the literary and translation point of view. During my research in the Chicano culture, I ran across Pat Mora. Her books for children fascinated me because of their actual themes (the cultural diversity and the defense of identity) and their beautiful illustrations. For this reason, I chose to translate seven of her books because I believe they could be an enrichment for children literature in Italy. The work consists of five chapters. The first one deals with the identity of Chicano people, their history, their literature and their language. In the second chapter, I outline Pat Mora’s profile. I talk about her biography and I analyze her most famous works. In the third chapter, I introduce the seven books for children to be translated and I point out their plots and main themes. In the fourth chapter, I present the translation of the books. The fifth chapter is the translation comment. I deal with the linguistic analysis of the source texts and the analysis of the target texts focusing on the choices made during the translation process.

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The morphological and functional unit of all the living organisms is the cell. The transmembrane proteins, localized in the plasma membrane of cells, play a key role in the survival of the cells themselves. These proteins perform a variety of different tasks, for example the control of the homeostasis. In order to control the homeostasis, these proteins have to regulate the concentration of chemical elements, like ions, inside and outside the cell. These regulations are fundamental for the survival of the cell and to understand them we need to understand how transmembrane proteins work. Two of the most important categories of transmembrane proteins are ion channels and transporter proteins. The ion channels have been depth studied at the single molecule level since late 1970s with the development of patch-clamp technique. It is not possible to apply this technique to study the transporter proteins so a new technique is under development in order to investigate the behavior of transporter proteins at the single molecule level. This thesis describes the development of a nanoscale single liposome assay for functional studies of transporter proteins based on quantitative fluorescence microscopy in a highly-parallel manner and in real time. The transporter of interest is the prokaryotic transporter Listeria Monocytogenes Ca2+-ATPase1 (LMCA1), a structural analogue of the eukaryotic calcium pumps SERCA and PMCA. This technique will allow the characterization of LMCA1 functionality at the single molecule level. Three systematically characterized fluorescent sensors were tested at the single liposome scale in order to investigate if their properties are suitable to study the function of the transporter of interest. Further studies will be needed in order to characterize the selected calcium sensor and pH sensor both implemented together in single liposomes and in presence of the reconstituted protein LMCA1.