ONTOLOGICAL MODEL OF A DATABASE OF INFORMATION-EDUCATIONAL PORTAL OF THE UNIVERSITY

According to the state program “Informational Society 2030”, it is planned to develop education on the basis of new progressive concepts of introducing the latest information technologies and scientific and methodological achievements into the educational process. In order to achieve goals, it is necessary to implement mobilization and effective use of staff and property and technical resources of the university. It is possible if there is purposeful modeling of the information and educational portal of the university. The choice and design of teaching technology are primarily determined by the type of students’ competencies and the characteristics of the planned learning outcomes for each level of competence (knowledge, skills, and experience). Constant improvement of EP content and educational technologies as a key factor of education services quality is a vital demand. The article considers the issues of the concept of ontology, IDEF-technologies and, based on the ontological model proposed in the article, the architecture of the database of the information and educational portal of the university is developed and classes and properties for the implementation of this model are defined, and a functional model of the university in IDEF0 is developed, which covers all types of university activities, integrates all information flows and forms a single information space

DEVELOPMENT OF AN INFORMATION AND EDUCATIONAL PORTAL OF DISTANCE LEARNING BASED ON EDUCATIONAL DATA MINING

Currently, there is an increase in demand for distance education programs, which actualizes the problems of organizing the educational process at universities using these technologies. The article highlights and describes the characteristic features and prospects of using the analysis of educational data in the information and educational portal of distance learning, in order to implement adaptive learning and learning in accordance with dynamically formed individual trajectories. The task is to create a fundamentally new information system of the university using the results of the analysis of educational data. One of the functions of such a system is to extract knowledge from the data accumulated during operation. Creating own system of this type is an iterative and time-consuming process that requires preliminary research and step-by-step prototyping of modules. The novelty lies in the fact that there is currently no methodology for developing such systems in Kazakhstan, so a number of experiments were conducted in order to collect data, select suitable methods for studying the collected data, and then interpret them. As a result of the experiment, the authors identified the sources of educational data available for analysis in the information environment of the university. The data of semester academic performance obtained from the Toraighyrov University information system, data obtained as a result of independent work of students and data obtained using specially developed Google-forms were taken as a basis. An information and educational portal was created for the automated collection, processing and analysis of educational data. Based on the study of students’ behavior, it becomes possible to form recommendations for teachers to improve the content and structure, as well as recommendations for the training of students. The data contained in the activity logs are examined to obtain information, search for dependencies by filtering relevant logs, structuring information from them and providing data in a form convenient for analysis and drawing conclusions. The data of the main types of events generated as a result of recording user actions in the learning management system and scenarios for using the results of the analysis of these data are considered. The elements of the software implementation of this system are described in detail, conclusions are made about the availability of the data sources used, and conclusions are drawn about the prospects for further development

Creating carbon nanotubes microenvironment in surfactant water solutions

© 2017 Trans Tech Publications, Switzerland. The infrared absorption spectra of aqueous dispersions of carbon nanotubes in the presence of surfactants and alkali metal salts in the frequency range from 1000 cm-1 to 3000 cm-1 have been studied. The possibility of controlling the characteristics of local environment of carbon nanotubes by varying external electrolyte and modulation the surfactant micelle structure has been shown

Calorimetric and Fourier transform infrared spectroscopic study of solid proteins immersed in low water organic solvents

Calorimetric heat effects and structural rearrangements assessed by means of Fourier transform infrared (FTIR) amide I spectra were followed by immersing dry human serum albumin and bovine pancreatic α-chymotrypsin in low water organic solvents and in pure water at 298 K. Enthalpy changes upon immersion of the proteins in different media are in a good linear correlation with the corresponding IR absorbance changes. Based on calorimetric and FTIR data the solvents were divided into two groups. The first group includes carbon tetrachloride, benzene, nitromethane, acetonitrile, 1,4-dioxane, n-butanol, n-propanol and pyridine where no significant heat evolution and structural changes were found during protein immersion. Due to kinetic reasons no significant protein-solvent interactions are expected in such systems. The second group of solvents includes dimethyl sulfoxide, methanol, ethanol, and water. Immersion of proteins in these media results in protein swelling and involves significant exothermic heat evolution and structural changes in the protein. Dividing of different media in the two groups is in a qualitative correlation with the solvent hydrophilicity defined as partial excess molar Gibbs free energy of water at infinite dilution in a given solvent. The first group includes the solvents with hydrophilicity exceeding 2.7 kJ/mol. More hydrophilic second group solvents have this energy values less than 2.3 kJ/mol. The hydrogen bond donating ability of the solvents also assists in protein swelling. Hydrogen bonding between protein and solvent is assumed to be a main factor controlling the swelling of dry solid proteins in the studied solvents. © 2001 Elsevier Science B.V

The influence of H-bonding on the enthalpies of solvation of proton acceptors in methanol

The influence of cooperative phenomena on the solvation of proton acceptors in methanol was studied. It was shown that solvation processes should be considered taking into account the dependence of the cooperative effect on the ability of the proton acceptor to form H-bonds with the solvent. A scheme for calculating the enthalpies of H-bond formation between proton acceptors and methanol associates is suggested. Copyright © 2005 by Pleiades Publishing, Inc

Structure and catalytic activity of α-chymotrypsin in solutions of gemini surfactants

The regulatory effect of gemini alkylammonium surfactants (GSurf) with the hexamethylene spacer varying in the length of alkyl radicals on the structure and catalytic activity of a-chymotrypsin was studied. A correlation between the activity of a-chymotrypsin and the length of the alkyl radical of GSurf was found. Gemini surfactants enhance the enzyme activity below the critical micelle concentration (CMC) and inhibit that above the CMC. The results of IR spectroscopy and the data on tryptophan fluorescence show that the interaction of GSurf with a-chymotrypsin induces changes in the protein structure differed in intensity. The most probable enzyme complexes with GSurf were characterized by the molecular docking method. © 2014 Springer Science+Business Media, Inc

Structure and properties of complexes of α-chymotrypsin with hydroxyl-containing gemini dicationic surfactants with a spacer moiety of varying length

© 2014 Pleiades Publishing, Ltd. The structure and properties of supramolecular complexes of α-chymotrypsin with hydroxyl-containing alkyl ammonium gemini surfactants (GSs) - α,ω-alkanedyl-bis(hydroxyethylmethylcetyl ammonium dibromides), with a polymethylene spacer of varying length have been studied. IR spectroscopy and tryptophan fluorescence data show that the interaction of GSs with α-chymotrypsin leads to changes of different intensity in the structural state of proteins. The most probable complexation mode of enzyme with GSs have been proposed by the molecular docking method. A correlation is found between the activity of α-chymotrypsin and the length of the GS spacer moiety. The enzyme activity correlates with the change in the substrate concentration in the aqueous phase of the surfactant micellar solution

Subunit Mobility and the Chaperone Activity of Recombinant αB-Crystallin

The comparison of the chaperone-like activity of native and covalently cross-linked human αB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism. Our data clearly demonstrate that the chaperone-like activity of α-crystallin is not only a surface phenomenon as was suggested by some researchers

Connection between dynamics and thermodynamics of liquids on the melting line

The dynamics of a large number of liquids and polymers exhibit scaling properties characteristic of a simple repulsive inverse power law (IPL) potential, most notably the superpositioning of relaxation data as a function of the variable TV{\gamma}, where T is temperature, V the specific volume, and {\gamma} a material constant. A related scaling law, TmVm{\Gamma}, with the same exponent {\Gamma}={\gamma}, links the melting temperature Tm and volume Vm of the model IPL liquid; liquid dynamics is then invariant at the melting point. Motivated by a similar invariance of dynamics experimentally observed at transitions of liquid crystals, we determine dynamic and melting point scaling exponents {\gamma} and {\Gamma} for a large number of non-associating liquids. Rigid, spherical molecules containing no polar bonds have {\Gamma}={\gamma}; consequently, the reduced relaxation time, viscosity and diffusion coefficient are each constant along the melting line. For other liquids {\gamma}>{\Gamma} always; i.e., the dynamics is more sensitive to volume than is the melting point, and for these liquids the dynamics at the melting point slows down with increasing Tm (that is, increasing pressure).Comment: 20 pages, 8 figures, 1 tabl

Calorimetric and FTIR-spectroscopic study of solvent effect on the state of dry solid bovine pancreatic α-chymotrypsin immersed in anhydrous organic solvents

Calorimetric heat effects and structural rearrangements accompanying the immersion of dry solid bovine pancreatic α-chymotrypsin in anhydrous organic solvents and water were measured at 298 K. It was found that the enthalpy and IR-absorbance changes being put together obey good linear correlation. According to the extent of their influence on the protein structure and thermodynamic state the solvents could be divided into two groups. The first group exhibiting nearly zero effects consists of carbon tetrachloride, benzene, nitromethane, acetonitrile, 1, 4-dioxane, n-butanol, n-propanol and pyridine. Dry solid protein is suggested to be stable in such media due to kinetic reasons. Immersion of the protein into a second group solvents, namely, dimethyl sulfoxide, methanol, ethanol, and in pure water as well, is followed by swelling of the protein and accompanied with significant exothermic enthalpy change and structural rearrangements. It was shown that attribution of the solvent to the first or the second group is determined by its thermody-namic hydrophilicity (partial excess molar Gibbs free energy of water in a given solvent at infinite dilution). The first group consists of liquids with thermodynamic hydrophilicities all above 2.7 kJ/mol. The thermodynamic hydrophilicities of the second group solvents are lower than 2.3 kJ/mol. At close hydrophilicities the presence of mobile protons in the solvent molecule sufficiently accelerates the solid protein swelling. It is deduced that thermodynamic hydrophilicity and proton donating ability could be principal factors controlling the stability of dry solid proteins and kinetics of swelling in liquids examined at room temperature