Abstract

Abstract
Solvent extraction is considered as a multi-criteria optimization problem, since several chemical species with similar extraction kinetic properties are frequently present in the aqueous phase and the selective extraction is not practicable. This optimization, applied to mixer-settler units, considers the best parameters and operating conditions, as well as the best structure or process flow-sheet. Global process optimization is performed for a specific flow-sheet and a comparison of Pareto curves for different flow-sheets is made. The positive weight sum approach linked to the sequential quadratic programming method is used to obtain the Pareto set. In all investigated structures, recovery increases with hold-up, residence time and agitation speed, while the purity has an opposite behaviour. For the same treatment capacity, counter-current arrangements are shown to promote recovery without significant impairment in purity. Recycling the aqueous phase is shown to be irrelevant, but organic recycling with as many stages as economically feasible clearly improves the design criteria and reduces the most efficient organic flow-rate.

Abstract
This paper presents the implementation of an algorithm for automatic identification of drops with different sizes in monochromatic digitized frames of a liquid-liquid chemical process. These image frames were obtained at our Laboratory, using a nonintrusive process, with a digital video camera, a microscope, and an illumination setup from a dispersion of toluene in water within a transparent mixing vessel. In this implementation, we propose a two-phase approach, using a Hough transform that automatically identifies drops in images of the chemical process. This work is a promising starting point for the possibility of performing an automatic drop classification with good results. Our algorithm for the analysis and interpretation of digitized images will be used for the calculation of particle size and shape distributions for modelling liquid-liquid systems.

Abstract
Molecular dynamics simulations is a valuable tool to study protein unfolding in silico. Analyzing the relative spatial position of the residues during the simulation may indicate which residues are essential in determining the protein structure. We present a method, inspired by a popular data mining technique called Frequent Itemset Mining, that clusters sets of amino acid residues with a synchronized trajectory during the unfolding process. The proposed approach has several advantages over traditional hierarchical clustering. © 2009 Springer Berlin Heidelberg.

Abstract
The recent increase in the number of complete genetic sequences freely available through specialized Internet databases presents big challenges for the research community. One such challenge is the efficient and effective search of sequence patterns, also known as motifs, among a set of related genetic sequences. Such patterns describe regions that may provide important insights about the structural and functional role of DNA and proteins. Two main classes can be considered: probabilistic patterns represent a model that simulates the sequences or part of the sequences under consideration and deterministic patterns that either match or not the input sequences. In this chapter a general overview of deterministic sequence mining over sets of genetic sequences is proposed. The authors formulate an architecture that divides the mining process workflow into a set of blocks. Each of these blocks is discussed individually. © 2010, IGI Global.

Abstract
The protein folding problem, i.e. the identification of the rules that determine the acquisition of the native, functional, three-dimensional structure of a protein from its linear sequence of amino-acids, still is a major challenge in structural molecular biology. Moreover, the identification of a series of neurodegenerative diseases as protein unfolding/misfolding disorders highlights the importance of a detailed characterisation of the molecular events driving the unfolding and misfolding processes in proteins. One way of exploring these processes is through the use of molecular dynamics simulations. The analysis and comparison of the enormous amount of data generated by multiple protein folding or unfolding simulations is not a trivial task, presenting many interesting challenges to the data mining community. Considering the central role of the hydrophobic effect in protein folding, we show here the application of two data mining methods - hierarchical clustering and association rules - for the analysis and comparison of the solvent accessible surface area (SASA) variation profiles of each one of the 127 amino-acid residues in the amyloidogenic protein Transthyretin, across multiple molecular dynamics protein unfolding simulations. © 2010, IGI Global.