Weaving networks in times of distancing: university, organizations and territory

En el artículo se abordan algunas de las acciones y las reflexiones que emergen del trabajo territorial realizado en el marco del Programa Economía Social, Solidaria y Popular (PESSyP) de la Facultad de Ciencias Sociales de la Universidad Nacional del Centro de la Provincia de Buenos Aires (UNICEN). Las autoras refieren al modo en el que el contexto de pandemia y de distanciamiento ha condicionado las modalidades con las que las organizaciones sociales, políticas, culturales y universitarias habitan el territorio y habilitan intervenciones integrales con los sujetos que allí participan.The article deals with some of the actions and reflections that emerge from the territorial work carried out within the framework of the Social, Solidarity and Popular Economy Program (PESSyP) of the Faculty of Social Sciences of the Universidad Nacional del Centro de la Provincia de Buenos Aires (UNICEN). The authoress refer to the way in which the context of the pandemic and distancing has conditioned the modalities with which social, political, cultural and university organizations inhabit the territory and enable comprehensive interventions with the social subjects that participate there.Facultad de Periodismo y Comunicación Socia

El comportamiento post-critico de las vigas de acero armadas con chapas delgadas

An advance of expositions concerning the method of ultimate strength or post-critical strength of steel beams reinforced with thin plates is presented. This method is being object of experimental researches at the Applied Mechanics and Structures Institute (IMAE) of the Mathematics and Engineering Faculty, National University, Rosario (Argentina).Se presenta un avance de planteamientos relativos al método de la resistencia última o resistencia post-crítica de vigas de acero armadas con chapas delgadas, el cual está siendo objeto de investigaciones experimentales en el Instituto de Mecánica Aplicada y Estructuras (IMAE) de la Facultad de Ciencias Exactas e Ingeniería de la Universidad Nacional de Rosario (República Argentina)

Universit\ue0 degli studi di Macerata

Sono illustrati i servizi di orientamento, tutorato e job placement delle 4 Universit\ue0 delle March

Application of Hansch’s Model to Capsaicinoids and Capsinoids: A Study Using the Quantitative Structure−Activity Relationship. A Novel Method for the Synthesis of Capsinoids

We describe a synthetic approach for two families of compounds, the capsaicinoids and capsinoids, as part of a study of the quantitative relationship between structure and activity

Fine grain thermal modeling and experimental validation of 3D-ICs

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Tuning chelation by the surfactant-like peptide A6H using predetermined pH values

We examine the self-assembly of a peptide A6H comprising a hexa-alanine sequence A6 with a histidine (H) “head group”, which chelates Zn2+ cations. We study the self assembly of A6H and binding of Zn2+ ions in ZnCl2 solutions, under acidic and neutral conditions. A6H self-assembles into nanotapes held together by a β-sheet structure in acidic aqueous solutions. By dissolving A6H in acidic ZnCl2 solutions, the carbonyl oxygen atoms in A6H chelate the Zn2+ ions and allow for β-sheet formation at lower concentrations, consequently reducing the onset concentration for nanotape formation. A6H mixed with water or ZnCl2 solutions under neutral conditions produces short sheets or pseudocrystalline tapes, respectively. The imidazole ring of A6H chelates Zn2+ ions in neutral solutions. The internal structure of nanosheets and pseudocrystalline sheets in neutral solutions is similar to the internal structure of A6H nanotapes in acidic solutions. Our results show that it is possible to induce dramatic changes in the self-assembly and chelation sites of A6H by changing the pH of the solution. However, it is likely that the amphiphilic nature of A6H determines the internal structure of the self-assembled aggregates independent from changes in chelation

Flow properties of caseinomacropeptide aqueous solutions: Effect of particle size distribution, concentration, pH and temperature

The purpose of this research was to evaluate the influence of particle size distribution, pH (5.0–9.0), concentration (1–15 g/100 g.) and temperature (5–60 °C) on the steady shear flow properties of caseinomacropeptide (CMP) aqueous solutions. These measurements were carried out by using a controlled stress rheometer. Flow curves were satisfactorily fitted by the Herschel-Bulkley model. CMP solutions exhibited Newtonian flow dependence, particularly at pH values 5.0–6.0. Non-Newtonian shear thinning behaviour was observed at pH 7.0–9.0. The concentration dependence on viscosity showed two different regimes of viscosity increase (dilute and concentrated). The overlap concentration was 8 g/100 g. The temperature dependent behaviour of CMP solutions fitted to the Arrhenius model regardless pH and concentration, and the calculated activation energy was 20 kJ/mol. The flow behaviour of CMP is explained in terms of peptide-peptide and peptide-water interactions. Based on these results, CMP molecules would form spontaneously micelles at pH > 4.5 in ultrapure water.Fil: Loria, Karina G.. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de Luján; ArgentinaFil: Aragón, Jimena C.. Universidad Nacional de Luján; ArgentinaFil: Torregiani, Sofía M.. Universidad Nacional de Luján; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; ArgentinaFil: Farías, María E.. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de Luján; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentin