Desarrollo de una aplicación usando LEAP

[ES]Hoy en día existen diferentes alternativas para interactuar con los ordenadores. Sin embargo, las más extendidas y utilizadas son el teclado y el ratón. En ambos casos resulta necesario que las manos del usuario entren en contacto con algún dispositivo, ya sea un teclado físico o un ratón. En determinadas circunstancias en las que la higiene de las manos es un factor importante, este hecho puede suponer un inconveniente. En este proyecto de fin de grado se ha desarrollado KVLeap, una aplicación de escritorio para los sistemas Windows, que usando el controlador Leap Motion, un dispositivo que detecta y rastrea la posición y los movimientos de las manos en el aire, permite interactuar con un ordenador sin que las manos del usuario tengan que entrar en contacto con ningún dispositivo.

Robust Sliding Mode Control for Tokamaks

Nuclear fusion has arisen as an alternative energy to avoid carbon dioxide emissions, being the tokamak a promising nuclear fusion reactor that uses a magnetic field to confine plasma in the shape of a torus. However, different kinds of magnetohydrodynamic instabilities may affect tokamak plasma equilibrium, causing severe reduction of particle confinement and leading to plasma disruptions. In this sense, numerous efforts and resources have been devoted to seeking solutions for the different plasma control problems so as to avoid energy confinement time decrements in these devices. In particular, since the growth rate of the vertical instability increases with the internal inductance, lowering the internal inductance is a fundamental issue to address for the elongated plasmas employed within the advanced tokamaks currently under development. In this sense, this paper introduces a lumped parameter numerical model of the tokamak in order to design a novel robust sliding mode controller for the internal inductance using the transformer primary coil as actuator.

Insights into mechanism kinematics for protein motion simulation

Background: The high demanding computational requirements necessary to carry out protein motion simulations make it difficult to obtain information related to protein motion. On the one hand, molecular dynamics simulation requires huge computational resources to achieve satisfactory motion simulations. On the other hand, less accurate procedures such as interpolation methods, do not generate realistic morphs from the kinematic point of view. Analyzing a protein's movement is very similar to serial robots; thus, it is possible to treat the protein chain as a serial mechanism composed of rotational degrees of freedom. Recently, based on this hypothesis, new methodologies have arisen, based on mechanism and robot kinematics, to simulate protein motion. Probabilistic roadmap method, which discretizes the protein configurational space against a scoring function, or the kinetostatic compliance method that minimizes the torques that appear in bonds, aim to simulate protein motion with a reduced computational cost. Results: In this paper a new viewpoint for protein motion simulation, based on mechanism kinematics is presented. The paper describes a set of methodologies, combining different techniques such as structure normalization normalization processes, simulation algorithms and secondary structure detection procedures. The combination of all these procedures allows to obtain kinematic morphs of proteins achieving a very good computational cost-error rate, while maintaining the biological meaning of the obtained structures and the kinematic viability of the obtained motion. Conclusions: The procedure presented in this paper, implements different modules to perform the simulation of the conformational change suffered by a protein when exerting its function. The combination of a main simulation procedure assisted by a secondary structure process, and a side chain orientation strategy, allows to obtain a fast and reliable simulations of protein motion.

Energetics and Structural Characterization of the large-scale Functional Motion of Adenylate Kinase

Adenylate Kinase (AK) is a signal transducing protein that regulates cellular energy homeostasis balancing between different conformations. An alteration of its activity can lead to severe pathologies such as heart failure, cancer and neurodegenerative diseases. A comprehensive elucidation of the large-scale conformational motions that rule the functional mechanism of this enzyme is of great value to guide rationally the development of new medications. Here using a metadynamics-based computational protocol we elucidate the thermodynamics and structural properties underlying the AK functional transitions. The free energy estimation of the conformational motions of the enzyme allows characterizing the sequence of events that regulate its action. We reveal the atomistic details of the most relevant enzyme states, identifying residues such as Arg119 and Lys13, which play a key role during the conformational transitions and represent druggable spots to design enzyme inhibitors. Our study offers tools that open new areas of investigation on large-scale motion in proteins.