Objetivo Aims: a) to study how the diverse biological functions of the recombinant lipocalin Major Urinary Protein (rMUP) including the ability to bind pheromones and odours and its pheromonal and allergen activity correlate with and are modulated by its structural and molecular dynamic features. b) to complete the training in Structural Biology focusing biomedical/biotechnological applications. a1) The request of new and more specific artificial sensors in food industry or environment control is increasing. MUPs bi ological activity is associated to the binding of hydrophobic molecules inside their pocket. A goal is to pin down the residues involved in binding and selectivity. Based on this knowledge we will design new mutants characterized by specific affinity for s elected compounds. a2) More than 20% of the population in industrialized countries suffer of allergies. MUPs are potent human allergens. Peptides encompassing portions of rMUP will be studied in search of the epitope(s) responsible for this pathological ef fect. This will allow to develop safer and more tolerable preparation for immunotheraphy. a3) The folding process of proteins is yet not understood. The beta-barrel lipocalins pose challenging questions since they may acquire non-native intermediate confor mational states. Unveiling the structure and dynamics of these states will be important to further the knowledge on the molecular mechanisms associated to protein folding and will allow to better understand how MUPs and lipocalins at large can carry out th ose so diversified biological functions. b1) To tackle biomedical or biotechnological problems it requires the combined use of structural biology tools: protein engineering and immunological techniques, multinuclear multidimensional NMR, fluorescence and c ircular dichroism spectroscopy. Therefore, this highly multidisciplinary project will provide the ground to complete, in the more comprehensive way, the training in basic and applied structural biology. Ámbito científico natural sciencesbiological sciencesbiochemistrybiomoleculesproteinsprotein foldingengineering and technologyelectrical engineering, electronic engineering, information engineeringelectronic engineeringsensorsmedical and health sciencesclinical medicineallergologynatural sciencesbiological sciencesmolecular biologystructural biologynatural sciencesphysical sciencesopticsspectroscopy Palabras clave Biotechnology Folding Human Health Protein Programa(s) FP6-MOBILITY - Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006 Tema(s) MOBILITY-2.3 - Marie Curie Incoming International Fellowships (IIF) Convocatoria de propuestas FP6-2004-MOBILITY-7 Consulte otros proyectos de esta convocatoria Régimen de financiación IIF - Marie Curie actions-Incoming International Fellowships Coordinador UNIVERSITY OF PARMA Aportación de la UE Sin datos Dirección Via Volturno 39 PARMA Italia Ver en el mapa Enlaces Sitio web Opens in new window Coste total Sin datos
