Polytechnic University of Catalonia

About: Polytechnic University of Catalonia is a education organization based out in Barcelona, Spain. It is known for research contribution in the topics: Finite element method & Population. The organization has 16006 authors who have published 45325 publications receiving 949306 citations. The organization is also known as: UPC - BarcelonaTECH & Technical University of Catalonia.

Artificial Intelligence and Environmental Decision Support Systems

Abstract: An effective protection of our environment is largely dependent on the quality of the available information used to make an appropriate decision. Problems arise when the quantities of available information are huge and nonuniform (i.e., coming from many different disciplines or sources) and their quality could not be stated in advance. Another associated issue is the dynamical nature of the problem. Computers are central in contemporary environmental protection in tasks such as monitoring, data analysis, communication, information storage and retrieval, so it has been natural to try to integrate and enhance all these tasks with Artificial Intelligence knowledge-based techniques. This paper presents an overview of the impact of Artificial Intelligence techniques on the definition and development of Environmental Decision Support Systems (EDSS) during the last fifteen years. The review highlights the desirable features that an EDSS must show. The paper concludes with a selection of successful applications to a wide range of environmental problems.

Application of predictive control strategies to the management of complex networks in the urban water cycle [Applications of Control]

Abstract: The management of the urban water cycle (UWC) is a subject of increasing interest because of its social, economic, and environmental impact. The most important issues include the sustainable use of limited resources and the reliability of service to consumers with adequate quality and pressure levels, as well as the urban drainage management to prevent flooding and polluting discharges to the environment.

Nonlinear equations for fractional Laplacians II: existence, uniqueness, and qualitative properties of solutions

Abstract: This paper, which is the follow-up to part I, concerns the equation $(-\Delta)^{s} v+G'(v)=0$ in $\mathbb{R}^{n}$, with $s \in (0,1)$, where $(-\Delta)^{s}$ stands for the fractional Laplacian ---the infinitesimal generator of a Levy process. When $n=1$, we prove that there exists a layer solution of the equation (i.e., an increasing solution with limits $\pm 1$ at $\pm \infty$) if and only if the potential $G$ has only two absolute minima in $[-1,1]$, located at $\pm 1$ and satisfying $G'(-1)=G'(1)=0$. Under the additional hypothesis $G"(-1)>0$ and $G"(1)>0$, we also establish its uniqueness and asymptotic behavior at infinity. Furthermore, we provide with a concrete, almost explicit, example of layer solution. For $n\geq 1$, we prove some results related to the one-dimensional symmetry of certain solutions ---in the spirit of a well-known conjecture of De Giorgi for the standard Laplacian.

Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction.

Abstract: The crystal structure of a synthetic peptide representing the major antigenic loop of foot-and-mouth disease virus (FMDV), complexed with the Fab fragment of a neutralizing monoclonal antibody raised against the virus, has been determined at 28 A resolution The peptide shows a high degree of internal structure with a nearly cyclic conformation The conserved Arg-Gly-Asp motif, involved in the viral attachment of aphtoviruses to cells, participates directly in the interaction with several complementarity determining regions of the antibody molecule The Arg-Gly-Asp triplet shows the same open turn conformation found in the reduced form of FMDV of another serotype and also in integrin binding proteins The observed interactions provide a molecular interpretation of the amino acid replacements observed to occur in mutants resistant to neutralization by this antibody The structure also suggests a number of restrictions to variation within the epitope which are imposed to keep the Arg-Gly-Asp motif in its functional conformation