Компетентностный подход и проблемы его реализации в высшей школе

Currently, the vocational education system is based on a competency-based approach, which considers the person»s ability to act productively in a professional situation rather than the amount of information learned as the result of education. The term «competency», as an indicator of the result of training, was introduced in the Russian Federation in 2009, with the introduction of the state educational standards for higher education of the first generation (Federal State Educational Standard), at the same time as the graduate students» competency model was introduced. Competence-based education implies competence-based orientation of both the content of the educational process and the methods of its implementation, as well as assessment procedures, means of assessing the quality of students» training, since the goals and the content of education, the organization of the educational process that are provided by educational standards, determine the results of education in the form of competencies. The implementation of the standards of competencies set in the Federal State Educational Standard of Higher Education in the actual learning process proved to be not so simple. Difficulties arise when relating the goals of education with the expected results, i.e., competencies. The difficulties are associated with the mismatch between the practical orientation of the competence-based approach and the existing subject-based orientation of the pedagogical practice. In the course of studying a specific discipline, the opportunity to fully form a speicfic competency, not a set of competencies specified by the Federal State Educational Standard, but also a specific competence, is small.However, the main difficulty is associated with the assessment of the level of competence formation. A competence-based approach requires measuring not only specific knowledge and skills of students, but an assessment of the qualities of the person him- or herself. However, the existing system for assessing the quality of education does not have the necessary assessment tools for this. This article discusses the issues of competence-based education in higher education, analyzes its features, and problems raleted to the assessment of the level of competence formation.В настоящее время система профессионального образования строится на компетентностном подходе, который в качестве результатов образования рассматривает не сумму усвоенной информации, а способность человека продуктивно действовать в профессиональной ситуации. Термин «компетенция», как показатель результата обучения, введен в РФ с 2009 г., с внедрением государственных образовательных стандартов высшего образования первого поколения (ФГОС), тогда же появляется компетентностная модель выпускника. Компетентностно-ориентированное образование подразумевает компетентностную ориентацию как содержания образовательного процесса и технологий его реализации, так и оценочных процедур, средств оценки качества подготовки обучающихся, поскольку цели и содержание образования, организация образовательного процесса, заданные образовательными стандартами, определяют результаты образования в форме компетенций. Переход от формулировок компетенций в ФГОС ВО к реальному процессу обучения оказался не таким простым. При соотнесении целей образования с предполагаемыми результатами - компетенциями возникают проблемы. Сложности связаны с несоответствием практической ориентированности компетентностного подхода и существующей предметной ориентацией педагогической практики. В ходе изучения конкретной дисциплины возможность сформировать в полной мере отдельную компетенцию не только набор компетенций, заданных ФГОС ВО, но и отдельную компетенцию - минимальна. Но основная сложность связана с диагностикой уровня сформированности компетенций. Компетентностный подход требует измерения не отдельных знаний, умений и навыков обучающихся, а оценки качеств самого человека. Однако существующая система оценки качества образования не имеет для этого необходимых оценочных средств. В представленной статье рассматриваются вопросы компетентностно-ориентированного образования в высшей школе, анализируются его особенности, проблемы диагностики уровня сформированности компетенций

Contribution of arginine-82 and arginine-86 to catalysis of RNases from Bacillus intermedius (binase)

To elucidate the functional role of Arg82 and Arg86 in the enzyme activity of binase, the extracellular ribonuclease of Bacillus intermedias, we used site-directed mutagenesis. On cleavage of various substrates the catalytic activity of binase mutant Arg86Ala is 2.7 x 103-7.7 X 103 times less than that of the native enzyme. The decrease in activity is determined preferentially by the decrease in the molecular rate constant k(cat) with a relatively small change of enzyme-substrate affinity, characterized by K(m). This is the expected result if Arg86 acts to lower the energy of a transition state of the reaction. The replacement of Arg82 by Ala causes a 519-fold activity decrease, depending on the substrate. We propose that this residue does not have a direct catalytic function in the molecular mechanism of the nase action and that the activity decrease of binase on the replacement of Arg82 by alanine is mediated by the effect of Arg82 on the pK of catalytic residues

Comparative study of thermostability and structure of close homologues - bamase and binase

Parameters of heat denaturation and intrinsic fluorescence of bamase and its close homologue, binase in the pH region 2-6 have been determined. The bamase heat denaturation (pH 2.85.5) proceeds according to the “all-or-none” principle. Bamase denaturation temperature is lower than that of binase and this difference increases from 2.5 °C at pH 5 to 7 °C at pH 3. Enthalpy values of bamase and binase denaturation coincide only at pH 4.5-5.5, but as far as pH decreases the bamase denaturation enthalpy decreases significantly and in this respect it differs from binase. The fluorescence and CD techniques do not reveal any distinctions in the local environment of aromatic residues in the two proteins, and the obtained difference in the parameters of intrinsic fluorescence is due to fluorescence quenching of the bamase Trp94 by the His 18 residue, absent in binase. Secondary structures of both native and denaturated proteins also do not differ. Some differences in the barnase and binase electrostatic characteristics, revealed in the character of the dipole moments distribution, have been found. © 1993 Taylor & Francis Ltd

Mutational analysis of the active site of RNase of Bacillus intermedius (BINASE)

To elucidate the functional role of some residues in the active site of binase, the extracellular ribonuclease of Bacillus intermedius, we used site-directed mutagenesis. On cleavage of various substrates the catalytic activity of binase mutant His101Glu is 2.0-2.7% of that for native enzyme. The decrease in activity is determined mainly by the decrease in molecular rate constant kcat with almost unchanged affinity of the enzyme for the substrate, characterized by KM. This is the expected result if His101 acts as an general acid, donating a proton to the leaving group on cleavage of a phosphodiester bond. The replacement of Lys26 by Ala causes a reduction in the enzyme activity to 13-33%, depending on the substrate. The activity decreases are due to changes in both kcat and KM for poly(I) and poly(A) but in kcat alone for GpA. In the latter case the effect is far less than that seen in the homologous mutation in the closely related enzyme, barnase. © 1994

Contribution of arginine-82 and arginine-86 to catalysis of RNases from Bacillus intermedius (binase)

To elucidate the functional role of Arg82 and Arg86 in the enzyme activity of binase, the extracellular ribonuclease of Bacillus intermedias, we used site-directed mutagenesis. On cleavage of various substrates the catalytic activity of binase mutant Arg86Ala is 2.7 x 103-7.7 X 103 times less than that of the native enzyme. The decrease in activity is determined preferentially by the decrease in the molecular rate constant k(cat) with a relatively small change of enzyme-substrate affinity, characterized by K(m). This is the expected result if Arg86 acts to lower the energy of a transition state of the reaction. The replacement of Arg82 by Ala causes a 519-fold activity decrease, depending on the substrate. We propose that this residue does not have a direct catalytic function in the molecular mechanism of the nase action and that the activity decrease of binase on the replacement of Arg82 by alanine is mediated by the effect of Arg82 on the pK of catalytic residues

Contribution of arginine-82 and arginine-86 to catalysis of RNases from Bacillus intermedius (binase)

To elucidate the functional role of Arg82 and Arg86 in the enzyme activity of binase, the extracellular ribonuclease of Bacillus intermedias, we used site-directed mutagenesis. On cleavage of various substrates the catalytic activity of binase mutant Arg86Ala is 2.7 x 103-7.7 X 103 times less than that of the native enzyme. The decrease in activity is determined preferentially by the decrease in the molecular rate constant k(cat) with a relatively small change of enzyme-substrate affinity, characterized by K(m). This is the expected result if Arg86 acts to lower the energy of a transition state of the reaction. The replacement of Arg82 by Ala causes a 519-fold activity decrease, depending on the substrate. We propose that this residue does not have a direct catalytic function in the molecular mechanism of the nase action and that the activity decrease of binase on the replacement of Arg82 by alanine is mediated by the effect of Arg82 on the pK of catalytic residues

Contribution of arginine-82 and arginine-86 to catalysis of RNases from Bacillus intermedius (binase)

To elucidate the functional role of Arg82 and Arg86 in the enzyme activity of binase, the extracellular ribonuclease of Bacillus intermedias, we used site-directed mutagenesis. On cleavage of various substrates the catalytic activity of binase mutant Arg86Ala is 2.7 x 103-7.7 X 103 times less than that of the native enzyme. The decrease in activity is determined preferentially by the decrease in the molecular rate constant k(cat) with a relatively small change of enzyme-substrate affinity, characterized by K(m). This is the expected result if Arg86 acts to lower the energy of a transition state of the reaction. The replacement of Arg82 by Ala causes a 519-fold activity decrease, depending on the substrate. We propose that this residue does not have a direct catalytic function in the molecular mechanism of the nase action and that the activity decrease of binase on the replacement of Arg82 by alanine is mediated by the effect of Arg82 on the pK of catalytic residues

Comparative study of thermostability and structure of close homologues - bamase and binase

Parameters of heat denaturation and intrinsic fluorescence of bamase and its close homologue, binase in the pH region 2-6 have been determined. The bamase heat denaturation (pH 2.85.5) proceeds according to the “all-or-none” principle. Bamase denaturation temperature is lower than that of binase and this difference increases from 2.5 °C at pH 5 to 7 °C at pH 3. Enthalpy values of bamase and binase denaturation coincide only at pH 4.5-5.5, but as far as pH decreases the bamase denaturation enthalpy decreases significantly and in this respect it differs from binase. The fluorescence and CD techniques do not reveal any distinctions in the local environment of aromatic residues in the two proteins, and the obtained difference in the parameters of intrinsic fluorescence is due to fluorescence quenching of the bamase Trp94 by the His 18 residue, absent in binase. Secondary structures of both native and denaturated proteins also do not differ. Some differences in the barnase and binase electrostatic characteristics, revealed in the character of the dipole moments distribution, have been found. © 1993 Taylor & Francis Ltd

Comparative study of thermostability and structure of close homologues - bamase and binase

Parameters of heat denaturation and intrinsic fluorescence of bamase and its close homologue, binase in the pH region 2-6 have been determined. The bamase heat denaturation (pH 2.85.5) proceeds according to the “all-or-none” principle. Bamase denaturation temperature is lower than that of binase and this difference increases from 2.5 °C at pH 5 to 7 °C at pH 3. Enthalpy values of bamase and binase denaturation coincide only at pH 4.5-5.5, but as far as pH decreases the bamase denaturation enthalpy decreases significantly and in this respect it differs from binase. The fluorescence and CD techniques do not reveal any distinctions in the local environment of aromatic residues in the two proteins, and the obtained difference in the parameters of intrinsic fluorescence is due to fluorescence quenching of the bamase Trp94 by the His 18 residue, absent in binase. Secondary structures of both native and denaturated proteins also do not differ. Some differences in the barnase and binase electrostatic characteristics, revealed in the character of the dipole moments distribution, have been found. © 1993 Taylor & Francis Ltd

Comparative study of thermostability and structure of close homologues - bamase and binase

Parameters of heat denaturation and intrinsic fluorescence of bamase and its close homologue, binase in the pH region 2-6 have been determined. The bamase heat denaturation (pH 2.85.5) proceeds according to the “all-or-none” principle. Bamase denaturation temperature is lower than that of binase and this difference increases from 2.5 °C at pH 5 to 7 °C at pH 3. Enthalpy values of bamase and binase denaturation coincide only at pH 4.5-5.5, but as far as pH decreases the bamase denaturation enthalpy decreases significantly and in this respect it differs from binase. The fluorescence and CD techniques do not reveal any distinctions in the local environment of aromatic residues in the two proteins, and the obtained difference in the parameters of intrinsic fluorescence is due to fluorescence quenching of the bamase Trp94 by the His 18 residue, absent in binase. Secondary structures of both native and denaturated proteins also do not differ. Some differences in the barnase and binase electrostatic characteristics, revealed in the character of the dipole moments distribution, have been found. © 1993 Taylor & Francis Ltd