Duward Shriver, Peter Atkins: Inorganic Chemistry, 5th edition, 2010, Oxford University Press

Stephen Lower: Chem1 virtual textbook a reference text for General Chemistry

http://www.chem1.com/acad/webtext/virtualtextbook.html

Laboratory exercises:

The evaluation will consist of two parts: reports from laboratory experiments, 4 points each (40 points maximum), and final written examination focused on the chemical principles of the performed syntheses (10 points). Only those students will be admitted to final examination who achieve at least 50 % of the points from laboratory work evaluation.

Lectures:

Final exam will consist of a 30-point test and oral examination for 20 points. Credits will not be assigned to a student, who will not earn at least 50% from laboratory work, and to student, who will not earn at least 50 % from final exam.

For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % of all points.

English

Lectures:

Composition of the matter; chemical reactions, formulae and equations; fundamental empirical laws; atomic structure; molecular structure – models of chemical bonding; Lewis theory; hybridization and valence bond theory; molecular orbital theory; bond polarity; electronegativity; oxidation number; ionic bond; hydrogen-bonding; van der Waals interactions. Principles of thermodynamics: Equation of state; state functions; internal energy; enthalpy; entropy; laws of thermodynamics; thermochemical laws; spontaneous processes; states of the matter; phase – phase transitions; disperse systems – mixtures, solutions; Raoult law – colligative properties. Solid state – structures. The principles of chemical kinetics: reaction rate and order; mechanism; catalysis; chemical equilibrium.

Electrolytic dissociation; acid-base theories; neutralization; pH; hydrolysis. Precipitation reactions; the solubility product. Photochemical and radical reactions. Oxidation and reduction.

Elements and their basic compounds: hydrogen; group 1-2 and group 13-18 elements; d-block elements; coordination bonding; basic stereochemistry; magnetic properties; organometallic compounds, basic biological functions of inorganic components.

Laboratory exercises:

Safety in a chemical laboratory. Basic laboratory glassware and operations. Laboratory experiments focused on: density, solubility, preparing solutions, crystallization, affecting chemical reactions, hydrolysis, oxidation and reduction reactions, synthesis of compounds and metals by redox reactions, heterogeneous reactions, proof reactions of inorganic cations and anions, synthesis of acids and basis, neutralization, amphoterism, coordination compounds.

This course covers the background and skills needed to understand the basic principles of chemistry. By the end of this course students should be:

• Able to understand the electronic structure of atoms, and acquires the basic knowledge on chemical bonding.

• Able to understand the molecular properties and the bulk properties of the matter. Basic principles in thermodynamics, chemical kinetics, chemical equilibrium, acid-base theories, and diverse types of chemical reactions.

• Able to understand basic properties of inorganic compounds of elements along all the groups of the periodic table.

• Skilled in basic nomenclature of inorganic compounds. Inherent to the course is training in solutions of chemical equations.

• Able to perform the basic laboratory experiments in the course of solving simple tasks related to the learned topic. Students will gain experience in basic laboratory techniques, synthesis of inorganic compounds and coordination compounds.

Form of Study: lectures and laboratory courses

Number of contact hours: 52

per week: 2 hours lectures + 2 lab courses per level/semester: 26/26

Form of the course: on-site learning

Lodish H., Berk A., Krieger M., Bretscher A., Amon A., Scott M.P. 2012. Molecular Cell Biology. 7th edition, ISBN-10: 142923413X

ISBN-13: 978-1429234139

Pollard T.D., Earnshaw W.C., Lippincott-Schwartz J. 2007. Cell Biology. 2nd Edition. ISBN-10: 1416022554

ISBN-13: 978-1416022558

Alberts B., Johnson A., Lewis J., Raff M., Roberts K., Walter P. 2007. Molecular Biology of the Cell. 5th Edition. ISBN-10: 0815341059

ISBN-13: 978-0815341055

Karp G. 2009. Cell and Molecular Biology: Concepts and Experiments. 6th Edition. ISBN-10: 0470483377

ISBN-13: 978-0470483374

Vesteg M., Krajčovič J. 2011. The falsifiability of the models for the origin of eukaryotes. Current Genetics 57: 367-390.

Practice - during the semester students will be evaluated on the basis of laboratory protocols, oral or written exams, lesson´s activity. Students who obtain at least 60% points can go to the final exam. Lecture - the final written examination. The final evaluation includes: (0.9 x% of the final exam) + (0.1 x% of the practice) = final %. A: 100% - 92%, B: 91% - 84%, C: 83% - 76%, D: 75% - 68%, E: 67% - 60%. The evaluation Fx will be awarded to a student who receives less than 60%.

English

The course will be held in winter semester only.

Definition of various cell types and their onthogenesis. Methods and techniques of cell investigation. Cell walls, plasmatic membrane, cytoskeleton. Endo-membrane cell system. Plastids and mitochondrion. Vacuoles, lysosomes, microbodies. Nucleus and cell cycle. Functional and morphological differentiation of animal cells and their cultivation. Mechanisms of differentiation, dedifferentiation, and regeneration of specific animal cell types. Cellular and non-cellular structures in microbiology. Functional and morphological differentiation of Protista cells. Eukaryotic cell as an integrative system of genetic compartments, its origin and evolution. Basic principles of cell signalling.

Students completing the course will gain knowledge of the structure, physiology, metabolism and cell function, the complete cell ontogeny - from creation through differentiation to their death. Students acquire the knowledge and skills in cultivation, processing, observation and analysis of cells that should be utilized after graduation practice in research, scientific research or clinical trials.

Form of Study: internal study (presence/online/combined)

Number of contact hours: 2 hours lecture and 1 hour practical per week

per week: 3 per level/semester: 39

Johnsonbaugh R., Pfaffenberger W.E., 2010: Foundations of mathematical analysis. Dover.

Apostol T.M., 1974: Mathematical Analysis, 2nd edition, Addison-Wesely.

Dettman J.W. 1968, Introduction to linear algebra and differential equations. Dover.

Grading Policy (Assessment/Evaluation): Grades will be based on the final exam test (contributing 100%). During the term students have to complete problems solutions, which will be defined in the frame of exercises and only those, who will finish all of these problems solutions will be accepted for the final examination. The course has a standardized grading system which is identified below:

A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

Syllabus/Indicative Content:

Basic concepts of algebra (statements, theorems, proofs), elementary sets and their properties.

Algebra of complex numbers. Fundamentals of linear algebra, matrices and their properties, basic matrix operations; determinant; systems of linear equations and methods of their solution (Gauss elimination method, Cramer’s rule). Elements of vector algebra, basic operations with vectors. Real functions of a real variable, elementary functions and their properties (graphs), inverse functions. Equalities and inequalities. Limit of the sequences and functions, basic rules for limits evaluation, continuity property of a function. Finite and infinite series. Derivative of real function of one variable – the definition, geometric significance, basic theorems; derivative of elementary function; derivatives of higher orders; differential of function and its practical use; Taylor’s series; the theorem on average value; L’Hôpital's rule. The course of a function – monotonous, convex, and concave functions, stationary and inflection points, local extremes, asymptotes. Indefinite integral, the primitive function - definition, methods of integration – integration by parts (per partes) and substitution method, integration of some rational functions, partial fractions decomposition. The concept of definite integral and its base properties; Newton-Leibniz formula; some applications and examples of definite integral – lengths of curve, surface of plane areas and volumes evaluation; infinite integrals.

Aims and Objectives:

This course covers selected topics from the basic theoretical background of mathematical analysis methods, used in the processing and interpretation of natural sciences experiments/datasets.

Johnsonbaugh R., Pfaffenberger W.E., 2010: Foundations of mathematical analysis. Dover.

Apostol T.M., 1974: Mathematical Analysis, 2nd edition, Addison-Wesely.

Dettman J.W. 1968, Introduction to linear algebra and differential equations. Dover.

Grading Policy (Assessment/Evaluation): Grades will be based on the final exam test (contributing 100%). During the term students have to complete problems solutions, which will be defined in the frame of exercises and only those, who will finish all of these problems solutions will be accepted for the final examination. The course has a standardized grading system which is identified below:

A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

Syllabus/Indicative Content:

The concept of ordinary differential equation, types of solutions, initial and marginal conditions. Differential equation of the 1st order with separable variables. Linear differential equations of the 1st and 2nd order with constant coefficients – homogeneous equations; Linear differential equations with constant coefficients and with a special right-hand side. Real function of several variables; the limit and continuity of function; partial derivatives; the total differential of the function of more variables and its use; local extremes of functions of two variables. Differential operators of scalar and vector fields: gradient, divergence, rotation, Laplace’s operator. Double integral, its geometric significance and properties, calculation of double and triple integral; line integrals. Fundamentals of statistical description of datasets and probability theory - basic statistical parameters, sorting intervals, central values (mean, median, modus) and moments, random variables and functions, sampling distributions (focused on normal Gaussian distribution), confidence intervals and tests, dispersion and correlation analysis.

Aims and Objectives:

This course covers selected topics from the basic theoretical background of mathematical analysis methods, used in the processing and interpretation of natural sciences experiments/datasets.

Form of Study: internal study (presence/online/combined)

Number of contact hours: 2 hours lecture and 1 hour practical per week

per week: 3 per level/semester: 39

Keller F.J., Gettys W.E., Skove M.J., 1993: Physics, classical and modern. McGraw-Hill.

Tipler P.A., Mosca G., 2003: Physics for Scientists and Engineers. W. H. Freeman.

Feynman C., Leighton R., Sands M., 2010: The Feynman Lectures on Physics, New Millennium Edition. California Institute of Technology.

Grading Policy (Assessment/Evaluation): Grades will be based on the final exam test

(contributing 100%). During the term students have to complete problems solutions, which will be defined in the frame of exercises and only those, who will finish all of these problems solutions will be accepted for the final examination. The course has a standardized grading system which is identified below:

A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

Syllabus/Indicative Content:

Introduction into classical vs. modern physics, fundamentals of mechanics (mass point, dynamics and kinematics, uniform motion, uniformly accelerated motion and motion with time-variable acceleration; Force, Newton’s laws, equation for the motion of a mass point, uniform circular motion; the work, kinetic and potential energy, conservation laws; Galileo's experiments, Keppler's laws, Newton’s gravitation law, center of mass of a system of particles and of a solid body, force moment, moment of inertia, Steiner’s theorem, the equations of movement for a solid body, movement in the gravitational field. Harmonic motion, damped and forced harmonic motion, combination of vibrations, wave equation, Huygens principle, interference of waves, Doppler effect; Introduction to the molecular physics and thermodynamics, ideal gas, Boltzmann’s distribution, pressure of the gas, absolute temperature, equation of state of an ideal gas, work of the gas, first law of thermodynamics, heat capacity, equipartition theorem. Electric charge, Coulomb’s law, intensity of electric field, electric dipole and its field, effect of electric field on a dipole, electric potential, capacity of the conductor, the energy of the electrostatic field of a condenser, dielectrics, polarization of a dielectric, permittivity of dielectric, the vector of electric induction. Ohm’s law, Kirchhoff’s laws and their use, Joule’s law; magnetic field, the vector of magnetic induction vs. magnetic intensity, magnetic permeability.

Aims and Objectives:

This course covers the seleted basic theoretical background of physics, involved into the state of the art interpretation of natural sciences models.

Form of Study: internal study (presence/online/combined)

Number of contact hours: 2 hours lecture and 1 hour practical per week

per week: 3 per level/semester: 39

Keller F.J., Gettys W.E., Skove M.J., 1993: Physics, classical and modern. McGraw-Hill.

Tipler P.A., Mosca G., 2003: Physics for Scientists and Engineers. W. H. Freeman.

Feynman C., Leighton R., Sands M., 2010: The Feynman Lectures on Physics, New Millennium Edition. California Institute of Technology

Grading Policy (Assessment/Evaluation): Grades will be based on the final exam test (contributing 100%). During the term students have to complete problems solutions, which will be defined in the frame of exercises and only those, who will finish all of these problems solutions will be accepted for the final examination. The course has a standardized grading system which is identified below:

A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

Syllabus/Indicative Content:

Elecromagnetic interaction: Lorentz’s force, speed filter and mass spectrometer; magnetic moment, Biot-Savart-Laplace's law; Ampere’s law, Faraday’s law of electromagnetic induction, Lorenz law; Maxwell’s equations in differential and integral form. Wave equation, electromagnetic waves, Poynting vector; properties of electromagnetic waves (according to Maxwell’s equations), refracting index, Fermat's principle, Snell’s law, refraction and reflection of light; Fundamental terms of geometrical optics (paraxial rays, refraction plain, focus), image by means of a plane, convex and concave mirror, lenses, lens equation, magnifying glass, microscope, spectrograph, electron microscope, double refraction, interference, diffraction, absorption and polarization of light, the laws of radiation of the black body (Wien’s, Rayleigh-Jeans and Planck’s laws), photoelectric effect, Einstein’s equation. Discrepancy of theory and experiment – motivation of introducing of quantum idea, new physical theories at the beginning of 20th century, theory of relativity, de Broglie wave, Bohr’s model of hydrogen atom, energetic levels, mathematical machinery of quantum mechanics, wave function and its probabilistic interpretation, operators of quantum mechanics, mean value of a quantity; Heisenberg’s uncertainty relations, Schrödinger equation (stationary and time- dependent), particle in a box, solution of the Schrödinger equation, stationary states; linear harmonic oscillator, the solution of Schrödinger equation, eigenvalues of the energy, eigenfunctions, Hermite's polynomials; potential barrier, tunneling, hydrogen atom, Laguerre polynomials, comparison with Bohr model; approximate solution of Schrödinger equation, solution for the hydrogen atom and its relation to the periodic table of elements; atomic nucleus and its models; elementary particles.

Aims and Objectives:

This course covers the seleted basic theoretical background of physics, involved into the state of the art interpretation of natural sciences models.

Form of Study: lecture / practical

Number of contact hours:

per week: 2/2 per level/semester: 26/26

Form of the course: on-site learning

Wessner D., Dupont CH., Charles T.C.: Microbiology John Wiley & Son Inc. 2013;

Hogg S., Essential Microbiology, 2nd Edition, John Wiley & Son Inc. 2013, Prescott Microbiology 11 ed., Willey, Sherwood, Woolverto eds 2021,

Koči, K. Practical Microbiology, Laboratory manual and Workbook (2021) Publishes by Comenius University in Bratislava, ISBN 978-80-223-5128-7

The final exam for students who completed Laboratory practice in Microbiology with a minimum grade E in the form of written test. The course has a standardized evaluating (grading) system: Grade A (100-92 %); B (91-84 %); C (83-76 %); D (75-68 %); E (67-60 %); FX (59-0 %).

English

History of microbiology, microbiology as one of the biological scientific disciplines, the subject of microbiology, methods used for study of microorganisms, research methods used in microbiology. Functional anatomy of prokaryotic and eukaryotic cells. Genetics of microorganisms, the structure of DNA, the structure of the gene, DNA replication, transcription, translation, mutations and mutagenesis, detection and isolation of mutants, gene transfer and recombination in prokaryotes and eukaryotes, extrachromosomal structures. The principles of taxonomy as scientific discipline, basic taxonomic classification of prokaryotic organisms Archaea and Eubacteria, classification of eukaryotic microorganisms: Fungi, Algae and Protozoa. Growth and nutrition of microorganisms, the growth curve, methods to measure the microbial growth, continuous cultivation, the impact of environmental factors on microbial growth, chemical and physical methods used in the control of the microbial growth. Metabolism of microorganisms, activation energy, catalysis, enzymes, oxidation, reduction, electron carriers, main energy stores in cells, release of energy in biological systems, fermentation, respiration, electron transport systems, carbon and electron flow in microbial cell. Microorganisms in the environment - soil, water, air. Biotic relationships between

microorganisms, types of symbiosis, antagonism, antibiosis, microbial biodegradation and biodeterioration. Microorganisms in biotechnology, industrially important fermentations, food

microbiology, microbiology of functional nutrition. Microorganisms as human pathogens, pathogenicity and virulence. Control of microbial growth, physical and chemical methods of sterilization, disinfection and disinfectants, anti-infective chemotherapeutics and antibiotics,

mode of actions of chemotherapeutics and antibiotics, resistance mechanisms to chemotherapeutics and antibiotics.

The course will provide general overview of the world of microorganisms - their diversity, activities, genetics, practical implications of their activities in medicine, industrial and food applications. Laboratory practice enables the students to acquire skills in basic microbiological methods.

Form of Study: lecture / practical

Number of contact hours:

per week: 2/2 per level/semester: 26/26

Form of the course: on-site learning

N. J. Dimmock A. J. Easton K. N. Leppard: N. J. Dimmock A. J. Easton K. N. Leppard: Introduction to modern virology, ISBN 978-1-119-97810-7 Fields Virology, ISBN-10: 1-4511-0563-0

Korsman et al., Virology an illustrated colour text, ISBN 9780443073670

Golais F.: Cellular Virology. 2021. Publishes by Comenius University in Bratislava, ISBN 978-80-223-5342-7.

Only students who have attended the exercises and passed them after a written exam with a minimum rating of E can pass the exam. The course has a standardized evaluating (grading) system: Grade A (100-92 %); B (91-84 %); C (83-76 %); D (75-68 %); E (67-60 %); FX (59-0 %).

English

Significant milestones in the history of virology. Position of viruses in the system of living matter, the principle of viral intracellular parasitism. Structure of viruses, symmetry of viral capsid. Phases of virus replication in infected cell, eclipsis characterization. Virus-cell interaction, productive, persistent, and latent virus infection, transformation of cells by viruses and tumours. Genetics of viruses, viral mutants, recombination, complementation, phenotype mixing. DNA viruses, cell replication and transformation. RNA virus replication. Retroviruses, transformation mechanisms. Basics of pathogenesis of viral infections. Basics of virus ecology. Transposons, retrotransposons, viroids, prions, replication mechanisms.

The course will provide students with basic knowledge of general virology, ie. j. on the structure, replication, pathogenesis, and ecology of viral diseases as well as on molecular biology of viral propagation and genetics of viruses. The exercise will enable students to acquire basic skills in the virological laboratory.

Snustadt, D.P., Simmons, M.J. (2011). Principles of genetics. John Wiley and Sons; 6th edition.

Hartwell, L.H., Hood, L., Goldberg, M.L., Reynolds, A.E., Silver, L.M., Veres, R.C. (2008). Genetics: From Genes to Genomes. 3rd Edition. McGraw-Hill, International Edition.

Russell, P.J. (2006). iGenetics: A Molecular Approach. 2nd Edition. Pearson/Benjamin Cummings. International Edition.

none

Grades will be based on (1) preliminary examinations at practicals during the semester (20% of the final mark) and (2) the final test covering the entire syllabus (80%). The course has a standardized grading system which is identified below:

A (92 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (85–91 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (77–84%): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (77–84%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60–68%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

Students' participation in practicals is obligatory

Lectures will cover the following areas of genetics:

Genetics as a biological discipline - Chromosome basis of inheritance - Mendelian inheritance - Genetic determination of sex - Deviations from mendelian inheritance - Linkage of genes and genetic recombination - Chromosomal aberations and their evolutionary and clinical implications - DNA structure and mechanism of replication - Anatomy and function of a gene - Mutations as a source of genetic variability - Gene expression I: Flow of genetic information from DNA to RNA - Gene expression II: Flow of genetic information from RNA to proteins - Gene expression III: Regulatory mechanisms in prokaryotes and eukaryotes - Methods in molecular genetics - Genetic analysis of prokaryotes - Population genetics - Inheritance of quantitative traits - Extrachromosomal inheritance - Genetic analysis of eukaryotic cell cycle and its implications for cancer - Genetic analysis of animal development - Comparative and evolutionary genomics.

Students will acquire a knowledge in classical genetics, cytogenetics, molecular basis of heredity, mechanisms involved in mutagenesis,

population and quantitative genetics, genetic basis of cancer and development, extrachromosomal inheritance and contemporary whole genome analyses and their implications for evolutionary biology and medicine.

Number of contact hours:

per week: 2 / 1 per level/semester: 26 / 13

on-site learning, online learning

D.A. Skoog, F.J. West, F.J. Holler, S.R. Crouch: Analytical Chemistry. An Introduction, Saunders Coll. Publ., 2000.

G. Schwedt: The Essential Guide to Analytical Chemistry, Wiley, New York, 1997.

R. Kellner, J.M. Mermet, M. Otto, Analytical Chemistry, John Wiley & Sons Australia, 2013.

Seminar – a maximum of 40 points, for elaboration and presentation of a seminar paper. Lecture – a maximum of 60 points, for the final test. The final grade will consist of evaluation of seminar and the final test from lecture, for a maximum of 100 points. For grade A it is necessary to obtain at least 92 points, for grade B at least 84 points, for grade C at least 76 points, for grade D at least 68 points and for grade E at least 60 points. The evaluation is the same for on-line learning.

English

The course is provided only in the winter semester. The course will switch to distance learning if enrollment falls below 5 students.

• Characteristics of separation methods, their function and significance in analytical, preparative, and industrial processes.

• General terms and parameters characterizing the scope of separation; terminology; distribution ratio, distribution constant, Nernst distribution law, chemical equilibrium in separation process. Interactions in separation systems. Calculations, thermodynamic and kinetic aspects of separation methods.

• One-stage separation methods, principle, technique, and application; separation of components by precipitation and co-precipitation. Sublimation, lyophilization. Electroprecipitation, electrolytic precipitation. Extraction separation in the system solid-liquid, liquid-liquid. Cloud point extraction – micellar systems. Membrane extraction. Simple distillation. Zone melting.

• Multistage separation methods and introduction to chromatographic methods. Multistage extraction, principle of continuous extraction. Multistage distillation. Chromatographic separations, classification according to various criteria. Theory of chromatographic phenomena, qualitative and quantitative chromatographic analysis.

• High-performance gas chromatography. Instrumentation. Separation mechanisms. Optimization of separation. Advanced techniques. Reaction chromatography, precolumn derivatization, vacant chromatography. Computer simulations and calculations.

• High performance liquid chromatography. Instrumentation, column vs planar techniques. Chromatographic phase systems. Advanced techniques. Computer simulations and calculations. Separation mechanisms. Pre-column and post-column derivatization (physical, chemical, and biological). Typical applications of chromatographic methods.

• Electroseparation methods. Principles, classification, parameters characterizing electroseparation. Concept of electrophoretic mobility, separation mechanisms, column vs. planar techniques, column coupling technique and detection. Zone electrophoresis. Separations in the free solution of carrier electrolyte. Separations in micelle-forming solutions, micellar electrokinetic chromatography. Electroosmotic flow. Instrumentation and practical use of computer simulation technique.

• Capillary isotachophoresis and isoelectric focusing. Basic principles, instrumentation and computer simulation technique. Separation, and analysis of proteins.

• Chip-based electroseparations. Miniaturization of separation columns and channels. Instrumentation and novel approaches to electroseparations. Advances and applications of chip-based electroseparations.

• Membrane separations. Principles, classification. Dialysis and electrodialysis, principle, instrumentation, and application. Ultrafiltration – application in analytical procedures. Validation of analytical methods with focus on separation methods.

• Solution of case studies from various areas of social and production practice. Typical application of separation methods in analytical procedures, preparative, and industrial procedures. Future trends in the development of separation methods.

Students will get acquainted with the position of separation methods within the system of scientific cognition of material reality and their essential need in generation of interpretable analytical signal. Objective is taught through a unified approach based on the concept of transport and distribution phenomena, which are applied in many modern separation methods. Separation methods are often the basis of chemical analysis methods. They are also base for qualitative evidence and quantitative measurement of characteristics or determination of chemical substances utilized in various human activities and related control, e.g., technological product analysis, bioanalysis, environmental analysis, clinical analysis, and diagnostics, etc. Students will gain information about the classification of analytical, preparative, and industrial separation processes and methods. The course also includes calculations in the field of separation sciences and solving case studies from social practice, which are discussed in the media.

Form of Study: lecture

Number of contact hours:

per week: 2 per level/semester: 26

Male, D. et al. (2021) Immunology, 9th edn AP Elsevier, ISBN: 978-0-7020-7844-6.

Punt, J. et al. (2019) Kuby Immunology, 8th edn, Macmillan, ISBN: 978-1-319-11470-1;

Abbas, A.K. et al. (2016): Basic Immunology, 5th edition, AP Elsevier, ISBN: 978-0-323- 39082-8.

Subject ends with a written exam. The course has a standardized evaluating (grading) system: Grade A (100-92 %); B (91-84 %); C (83-76 %); D (75-68 %); E (67-60 %); FX (59-0 %).

English

The immune system. Cells of the immune system. Tissues and organs of the immune system. Cell adhesion molecules and leukocyte migration. Cytokines. Mediators of immune responses. Complement. Inflammation. Major histocompatibility complex molecules. Structure of immunoglobulins and T-cell receptors. Antigens and their recognition. Cellular immune responses. Cooperation cells in antibody formation. Regulation of immune responses, immune tolerance. Immune system and microorganisms. Immune defence against viruses, bacteria, fungi, protozoa and parasitic worms. Immunoprophylaxis. Vaccination. Antitumor immunity. Immunopathological processes. Hypersensitivity reactions (type I to V). Autoimmunity. Overview of autoimmune diseases. Basic characteristics of immunodeficiencies. Primary and secondary immunodeficiencies.

Immunology is one of the most dynamic disciplines that affect the clinical virology and microbiology. Lectures in immunology give students a basic understanding of the immune system, its anatomy, structure, and function in the human body. The aim of the lectures is also acquainted students with basic immunological processes occurring in the body during infection of various infectious pathogens.

Type of activities: lecture

Number of hours:

per week: 2 per level/semester: 26

Form of the course: on-site learning / online

Groves M. J., 2006: Pharmaceutical biotechnology-second edition, CRC press, 396 pp.

Smith J. E., 2009: Biotechnology,Cambridge university press, 280 pp.

Walsh, G.., 2007: Pharmaceutical biotechnology. John Wiley and Sons Ltd, 465 pp.

Demain A. L., Davies J. E., 1999: Manual of industrial microbiology and biotechnology,

American society for microbiology, 830 pp.

Friedman Y. 2006: Building Biotechnology, Thinkbiotech, 306 pp.

Grades will be based on a final written examination, which will consist of two areas – each 100% (see Learning Outcomes section). At least 50% will need to be obtained from each area. The final grade will be the average of the evaluation of both parts: A (92 – 100%) B (84 – 91 %) C (76 –83) D (68 –75%) E (60 – 67%) Fx (under 60%)

English

Introduction to biotechnology, definition of the terms, development of biopharmaceuticals, preclinical and clinical trials and protection of the data thereof, registration process of drugs in USA and Europe and essential collection of the documents associated with it, ethic committee, good manufacturing practice, European directorate for the quality of medicines and healthcare and pharmacopoeia, and protection of intellectual property rights. Production process of biopharmaceuticals, down-stream and up-stream processes, product quality control, stabilization of biopharmaceuticals and drug formulation, stability testing, standards for injection water, clean room categories and endotoxins, process waste and its disposal. Production organisms and expression system thereof, basic features of expression systems from bacteria to transgenic animals. Examples of important biopharmaceuticals produced by selected production organisms: interferons, interleukins, tumor necrosis factors, hematopoietic growth factors, growth factors, hormones, blood product, enzymes, antibodies, vaccines and adjuvants. Basics in environmental biotechnology, bioprospecting, bioremediation, biosensors, biotechnology in waste disposal, biodegradable plastics produced by microorganismsBasics in food biotechnology, genetically modified organisms in food biotechnology, single cell protein.

After the course, students should understand basic principles of biotechnology and its impact on society in general and be able to orientate in the field of biotechnology information and be able to accumulate and transform the information into logical outputs in the form of presentation. An acquired knowledge will be in two areas:

1. Biopharmaceutical production and corresponding legislation: • Legislative framework of pharmaceutical biotechnology and process of drug registration in Europe and USA.

• Production process of biopharmaceuticals and required technological and non-technological

necessities for production.; Fundamental organisms used for production of biopharmaceuticals

and employed expression systems.

2. Basic potential application of classical and modern biotechnology in solving of environmental and food problems and perspectives of modern biotechnology in the fields.

Type of activities: seminar

Number of hours:

per week: 2 per level/semester: 26

Form of the course: on-site learning

Specifically, as recommended by supervisor

Assessment will be based on the student's work throughout the semester. A Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D Less acceptable work, relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

Formal requirements for Bc. work at Comenius University, Rector's Directive. Sources of professional literature, work with databases. Principles of oral presentation of professional results. Publishing in professional journals, parameters of scientific journals quality, predatory journals. Progress reports of writing Bc. thesis and about communication with supervisors. Participants are expected to read and provide constructive feedback to the draft chapters.

Students will get acquainted with the basics of professional presentation. They will also get familiar with professional and formal requirements that are placed on the final theses and their defence in the bachelor's degree program of biochemistry. They will learn to process knowledge in the form of research, present an overview of scientific work in writing and through a lecture. The Bachelor seminar offers an opportunity for Bachelor students to present and discuss their work in progress.

Form of Study: seminar

Number of contact hours:

per week: 2 per level/semester: 26

Form of the course: on-site learning

Research papers related to the topic of bachelor thesis.

Active participation in the course is mandatory. Final grade is based on the quality of 2 presentations and student's ability to discuss their own and another research projects, as well as original research papers in the field.

Standardized grading system is identified below:

A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyse, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80%): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyse, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyse or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

This course is available only in summer semester.

Bachelor students present and discuss their work in progress. During the semester each student prepares two presentations. The one will refer to a selected or assigned research paper from the field of biology or chemistry. In the second presentation, students introduce the aim and highlight the main topics of their Bachelor thesis. All students are expected to join the discussion and provide feedback to presenting colleagues.

Bachelor seminar is designed to improve presenting skills and abilities to discuss obtained knowledge and to develop independent thinking in bachelor students. Students are required to present a progress in writing of their Bachelor thesis; they are encouraged to discuss any formal or scientific issues that rise during preparing of their work.

Specifically, as recommended by supervisor

Grading Policy (Assessment/Evaluation): Grades will be based on the final Bachelor thesis report (contributing 100%), which has a standardized grading system identified below: A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80%): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

The course in individual and consultative design offers an opportunity to complete and submit Bachelor thesis as well as to present and discuss work in progress. Participants are expected to read and provide constructive feedback to the draft chapters. There is no specific syllabus for this type of seminar. The content is given by the topic of the Bachelor thesis.

The Bachelor thesis serves to improve skills and abilities for independent research in final Bachelor thesis. The primary task is to prepare own Bachelor thesis which will be discussed and reviewed individually by each supervisor.

Form of Study: lecture

Number of contact hours:

per week: 2 per level/semester: 26

Form of the course: on-site learning

Fox SI: Human Physiology, 14th ed. McGraw-Hill Education, New York, USA, pp 832, 2016.

Constanzo LS.: Physiology, 6th ed. Elsevier, Philadelphia, USA, pp 528, 2018.

Koeppen BM & Stanton BA: Berne & Levy Physiology. Elsevier - Health Sciences Division, St Louis, USA, pp 864, 2008.

Sherwood L et al: Animal Physiology: From Genes to Organisms, 2nd ed. Cengage Learning, Inc, Florence, USA, pp 840, 2013.

Final exam is in the form of a written test. Student is evaluated by A (if obtains at least 90% of total score), B (if obtains at least 82% of a total score), C (if obtains at least 75% of a total score), D (if obtains at least 68% of a total score), E (if obtains at least 60% of a total score) and Fx (if obtains less than 60% of a total score).

This course is available only in winter semester and will be opened if at least 3 students enrol.

Principle of Homeostasis; Cell Physiology; Membrane Transports; Membrane Potential and Cell Signalling; Neuronal Physiology; Gastrointestinal Physiology; Physiology of the Blood; Immune Mechanisms; Cardiovascular Physiology; Respiratory Physiology; Physiology of the Kidneys; Endocrine Physiology; Reproductive Physiology

The course brings the background needed to understand the fundamental processes and mechanisms that control the various body functions. By the end of this course students should be able to understand general aspects of animal and human physiology, to integrate concepts and approaches from regulatory mechanisms from the level of animal cell to the entire organism, and to understand control systems, including cardiovascular, gastrointestinal, respiratory, excretory, immune, reproductive, endocrine and nerve systems.

Form of Study: lecture / seminar

Number of contact hours:

per week: 2 / 1 per level/semester: 22 / 11

on-site learning

1. Berg, J. M, Tymoczko, J. L, Gatto, Jr., G. J., Stryer, L. (2015). Biochemistry, 8th Edition, W. H. Freeman and Company (The 7th edition is also sufficient).

2. Nelson, D. L., Cox, M. M. (2017). Lehninger Principles of Biochemistry, 7th Edition, W. H. Freeman, Macmillan Learning (The 6th edition is also sufficient).

Presence at seminars. Obtaining 50% of both parts is a prerequisite for successful completion of the subject. Assessment from the seminar will be 30% and written test at the end of Lecture course 7 0% of the total subject assessment. For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % from all points.

English

The course is provided only in the summer semester.

Regulation of gene expression, initiation of RNA transcription, gene regulatory proteins (a.k.a. transcription factors) and their binding to DNA, DNA structures as target for regulatory proteins (e.g. helix-turn-helix, leucine zipper, helix-loop-helix, zinc fingers).

· Biological relevance of DNA and RNA modification - methylation of CpG islands, N6-methyladenosine in mRNA, tRNA modifications and translation.

· Carbohydrates – Cell wall polysaccharides of bacteria and plants: structure, function, biosynthesis. Carbohydrates in health and disease.

· Structural components of proteins - amino acids - properties, peptide bond formation, reactions

in biochemistry - thermodynamics of chemical reactions, the transition state of a chemical reaction, non-covalent interactions.

· Lipids - Functional roles of lipids in membranes. Synthesis of phospholipids and sterols. ntramembrane and intermembrane lipid transport. Lipid modification of proteins. Approaches

to lipid analysis.

· Steady-state kinetics of the one substrate reaction; time course of enzyme-catalyzed reactions.

Michaelis-Menten equation and its transformation, enzyme inhibition. Experimental measurement of enzyme activity - measuring the initial speed; detection methods, factors affecting the rate of enzyme reaction, enzyme stability. Enzyme reactions with multiple substrates.

· Mechanisms of enzyme catalysis. Examples of mechanisms of enzymatic catalysis and its regulation - serine proteases, aspartic acid proteases, glutathione reductase, hexokinase.

· Enzyme regulation - zymogens, isoenzymes, covalent modification, allosteric enzymes. Enzyme Engineering - stabilization of enzymes, change the properties of enzymes by gene manipulations.

Seminars

· The theme of seminar renders the syllabus of lecture. Seminars focus on solving of practical problems related to corresponding lecture.

1. Insight into various types of gene expression regulations.

2. Biological relevance of DNA and RNA modification.

3. Biochemistry of macromolecules: lipids, proteins, and carbohydrates. Synthesis, turnover, functions, and analysis.

4. Thermodynamic of enzymatic reactions.

5. Enzyme catalysis. Michaelis-Menten equation.

6. Enzyme regulations.

Form of Study: practical

Number of contact hours:

per week: 2 per level/semester: 26

Form of the course: on-site learning

Sherwood L et al: Animal Physiology: From Genes to Organisms, 2nd ed. Cengage Learning, Inc, Florence, USA, pp 840, 2013.

Study materials for practical lessons.

Successful completion of this course requires mandatory participation in practical lessons and an achievement at least 60% score from each of 2 written tests. Moreover, students are evaluated by their activity and laboratory reports, which must submit from each practical lesson. Students are evaluated by A (if obtains at least 92% of a total score), B (if obtains at least 84% of a total score), C (if obtains at least 76% of a total score), D (if obtains at least 68% of a total score), E (if obtains at least 60% of a total score) and Fx (if obtains less than 60% of a total score).

This course is available only in winter semester and will be opened if at least 3 students enrol.

The syllabus follows the lectures from Animal and Human Physiology. The main themes are as follows: Biological membranes (osmosis and diffusion), Physiology of digestion (proteins, lipids, saccharides), Blood, Blood pressure monitoring, Body temperature and Thermoregulation, Excretion, Respiration, Reflexes, Physiology of the sensory system.

Students will learn and obtain practical laboratory skills through performing different laboratory tasks illustrating basic physiological principles. e.g. observation of osmosis and diffusion in various models, proof reactions for presence of proteins, lipids and saccharides, blood typing, measurement of lung volumes, quantitative measurement of oxygen dissolved in water by Winkler method, etc. By the end of this course, students will be able to perform, analyse and report on experiments and observations in physiology.

Type of activities: lecture

Number of hours: per week: 4 per level/semester: 52

Form of the course: on-site learning

Nelson, D. L. a Cox, M.M. (2017) Lehninger Principles of Biochemistry, W.H. Freeman;

Berg J.M., Tymoczko J.L., Gatto G.J. a Stryer L. (2019) Biochemistry, MacMillan

The exam will consist of the written part (A) and the oral part (B).

Part A (70%):

14 questions (multiple choice, short answer)

7 correct answers are needed to qualify for the part B

Part B (30%):

3 questions

Failure to answer at least one of these questions means failing the exam.

Final grade: 100-90% A, 89-80% B, 79-70% C, 69-65% D, 64-60% E, Fx-less then 60%

English

1. Carbohydrates. Classification, physico-chemical and biological properties of carbohydrates. Stereochemistry: configuration, conformation, enantiomer, epimer, diastereomer, mutarotation, α-, β-anomers. Glycosidic bond. Oligosaccharides and polysaccharides. Structural polysaccharides, storage polysaccharides - bonds, structures.

2. Amino Acids and Proteins. General formula of AA, classification of AA, formulas of AA, optical activity, spectroscopic properties of AA, acid-base properties of AA, zwitterions, amphoteric character of AA, isoelectric point, structure and properties of the peptide bond. Three-dimensional structure of proteins - primary, secondary (α-helix, β-pleated sheet, β-turn), tertiary, quaternary; bonds (interactions) and functional groups implied in these structures. Classification of proteins according to structure and solubility (fibrous, globular, membrane proteins). Biological functions of proteins, native conformation, denaturation, renaturation.

3. Enzymes. Holoenzyme, apoenzyme, cofactor, coenzyme, prosthetic group. Classification of enzymes. Active site, specificity of enzymes. Mechanism of action of enzymes – “lock and key”, “induced fit”. Activation energy, transition state. Enzyme kinetics, Michaelis - Menten equation, parameters KM and Vmax; enzyme inhibition - irreversible, reversible - competitive, uncompetitive, mixed. Regulation of enzyme activity - allosteric modification, covalent modification, regulatory proteins, proteolytic cleavage (zymogens).

4. Lipids and Membranes. Functions of the lipids. Structure and properties of fatty acids. Storage lipids: triacylglycerols (fats, oils), waxes. Membrane lipids: glycerophospholipids, sphingolipids, sterols. Amphipathic character of some lipids, aggregated forms of lipids - micelles, bilayers. Biological membranes, membrane proteins, fluid mosaic model.

5. Introduction to metabolism. Sources and transformations of energy in the biosphere. Laws of thermodynamics (1st and 2nd). Chemical energy - enthalpy, free (Gibbs) energy, entropy. Endergonic, exergonic reactions. Carriers of chemical energy. ATP – its role and production in the living systems (substrate-level phosphorylation, oxidative phosphorylation, photophosphorylation). Catabolic and anabolic metabolic pathways. Energy relationships between catabolic and anabolic pathways. Oxidation of biomolecules.

6. Metabolism of glucose. Glucose as a source of metabolic energy. Glycolysis - significance, localization, 2 phases of glycolysis, individual reactions, intermediates and enzymes of glycolysis. Fate of pyruvate. Lactic fermentation, alcoholic fermentation. Gluconeogenesis - significance, substrates, three unique gluconeogenetic steps (4 enzymes), localization. Cori cycle, transfer of lactate from muscle to liver, formation of glucose from lactate. Pentose phosphate pathway: significance, formation of NADPH, ribulose-5-phosphate, reactions catalyzed by dehydrogenases, isomerase, epimerase, transaldolases, transketolase.

7. Krebs cycle. Glyoxylate cycle. Formation of acetyl-coenzyme A from pyruvic acid. Krebs cycle as a source of energy and biosynthetic precursors, cellular localization of the cycle. Krebs cycle reactions, individual intermediates and enzymes. Amphibolic character of the citrate cycle, anaplerotic reactions (pyruvate carboxylase). Glyoxylate cycle - importance for plants and bacteria, localization, enzymes.

8. Metabolism of fatty acids. Fatty acids as a source of metabolic energy. Fats digestion - bile acids, lipases, chylomicrons. The fate of fatty acids in muscle and adipose tissue. Release of fatty acids from adipose tissue and their transfer to tissues. β-oxidation of fatty acids - localization in the cell, transfer of fatty acids to mitochondria (carnitine function). b-oxidation reactions, formation of acetyl-coenzyme A. Fate of acetyl-coenzyme A - entry into the citrate cycle. Fatty acid biosynthesis - comparison with β-oxidation, reactions. Sources of NADPH. Transport of fat and cholesterol in humans, roles of lipoproteins.

9. Oxidative phosphorylation. Structure and functions of mitochondria. Composition and function of the respiratory chain, electron transporters - cytochromes, iron-sulfur proteins, ubiquinone, flavoproteins. The source of electrons entering the respiratory chain. Electron transfer in the respiratory chain (complexes I, II, III, IV, cyt c, ubiquinone). Proton gradient. ATP synthesis, ATP-synthase. Chemiosmotic theory. Alternative use of proton gradient - thermogenesis, movement of bacteria, transport of metabolites.

10. Photosynthesis. Structure and function of chloroplasts. Pigments and their role in photosynthesis. Photochemical reaction centers. Electron transfer by photosystems I and II. Non-cyclic and cyclic photophosphorylation. Photolysis of water. Production of NADPH. Synthesis of carbohydrates during photosynthesis. Three stages of CO2 assimilation. Basic reactions and function of Calvin cycle.

11. Degradation of amino acids and urea cycle; metabolism of nucleotides. Deamination, transamination and decarboxlation of amino acids. Amino-transferases. Fate of NH4+ in various organisms. Urea cycle and its interconnection with citric acid cycle. Biosynthesis of ribonucleotides and deoxyribonucleotides de novo and by salvage reactions. Degradation of nucleic acids. Degradation of purine and pyrimidine bases.

12. Nucleotides and Nucleic Acids. Nitrogenous bases found in RNA and DNA. Nucleosides and nucleotides – their structure and components (nucleobases, sugar, phosphoric acid). Structure of deoxyribonucleic acid: (i) primary structure; (ii) secondary structure and its discovery; (iii) ABZ forms of the secondary structure; (iv) another alternative forms of the secondary structure (cruciform, G-quadruplex, Hoogsteen base pairing); (v) tertiary structure (supercoils, topoisomerases). DNA replication enzymes and the rules – semiconservative, bidirectional, semidiscontinuous (Okazaki fragments). DNA denaturation. Chromosome structure in eukaryotes – the nucleosome and nuclear DNA packing levels. DNA/RNA differences. Structure of ribonucleic acid: (i) primary structure; (ii) secondary structure; (iii) tertiary structure. Various forms of RNA serving different functions in cell – mRNA, rRNA, tRNA, snRNA, snoRNA, ncRNA.

13. Transfer of genetic information. Transcription: General features of transcription, prokaryotes and eukaryotes comparison. Transcription in prokaryotes: initiation, elongation, termination. Transcription in eukaryotes: initiation, elongation, termination and introduction to the mRNA processing. Inhibitors of transcription in prokaryotes and eukaryotes. Genetic code and Translation: Structure of tRNA. Function of tRNA in translation. Genetic code, its features (triplet code, continuous, not overlapping, degenerate, unambiguous, universal). Decoding of the standard genetic code. Natural and unnatural variations in the standard genetic code. Loading the tRNAs and aminoacyl-tRNA synthetases. Codon-Anticodon pairing. Ribosome, its structure, prokaryotes and eukaryotes comparison. Translation – protein synthesis mechanism and stages: initiation, elongation, termination. Translation elongation cycle three principal steps: codon-directed binding, peptide bond formation (ribosome is ribozyme), translocation. Molecular mimicry. Inhibitors of protein synthesis.

14. Recombinant DNA, artificial manipulation with Nucleic acids. Cloning of DNA: history, plasmids, restriction enzymes, ligases, linkers and polylinkers, shuttle vectors. Genomic gDNA library and complementary DNA cDNA library. Preparation of gDNA library and cDNA library. Particular DNA segment identification by hybridization – Southern blotting. Colony hybridization. Polymerase chain reaction – PCR cycle stages: heating, cooling, polymerization. DNA primary structure determination – DNA sequencing methods: Sanger method and Maxam-Gilbert chemical cleavage method.

Students are introduced to biochemical processes taking place in living organisms. After completing the course they will understand chemical structure of biomolecules in relation to their functions, they will comprehend basics of enzyme catalysis and intermediary metabolism.

Form of Study: lectures, seminar, practicals

Number of contact hours: 2 h lectures, 2 h seminars, 1 h practicals

per week: 5 per level/semester: 45

J. B. Lambert: Organic Structural Spectroscopy, Prentice Hall, New Jersey, 1998.

Course will be evaluated by a written test. For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % of all points. Credits will not be assigned to a student, who will not earn at least 60% overall from final exam.

English

1. Overview of molecular spectroscopy methods. Basic principles. Vibrational spectroscopy.

Vibrations of molecules, infrared and Raman spectroscopy. Experimental methods.

2. Vibrational spectroscopy, group frequencies and factors influencing group frequencies.

Vibrational spectra in structural analysis. Vibrational circular dichroism.

3. Electronic spectroscopy. Physical principles. Electronic spectra of fundamental classes of organic

compounds. Measurement of UV-VIS spectra and their use in structural analysis. Fluorescence and

phosphorescence. Optical rotatory dispersion. Circular dichroism. Cotton efect.

4. NMR spectroscopy,fundamental physical principles, magnetic properties of nuclei. Survey of

spectral parameters.

5. Chemical shift. Factors influencing chemical shift. 1H and 13C chemical shifts.

6. Spin-spin interaction, H-H, C-H coupling constant and chemical structure. First and second order

spectra. Chemical and magnetic equivalency. Spectral analysis.

7. Relaxation, reactions on NMR time scale. Double resonance experiments. Nuclear Overhauser

effect. Edited spectra.

8. 1D NMR experiments with complex pulse sequences. Two dimensional NMR. 2D J-resolved

spectra. Homonuclear and heteronucklear chemical shift correlation. Through space correlation.

9. NMR spectroscopy in biochemistry and medicine. Solid state NMR. NMR imaging (MRI).

10. Principles of mass spectrometry. Types of MS spektrometry, consequence of isotopic ions,

resolution of MS spectra, high resolution MS. Types of ionization, mass analysis.

11. General principles of ion-fragmentation. Mechanisms of fragmentations and rearrangements of

ions. Interpretation of MS spectra, use in structural analysis.

12. Electron spin resonance (ESR), electron spin-levels in magnetic field g-factor. hyperfine

structure. Laser spectroscopy. Time resolved spectroscopy.

13. Combined use of spectral methods. Solving structure of compound by spectral methods

The aim of the course is to introduce basic principles of molecular spectroscopy and its applications

in structure determination. The course deals with theoretical principles of spectroscopy and with

factors influencing spectral characterics and their use in structural analysis of molecules. Primary

focus is on most important methods of molecular spectroscopy such as NMR, MS, IR, UV-VIS, but

principles and examples of application of other special techniques are also given. Basic

experimental techniques are introduced to students. Seminars are devoted to solving spectra.

Type of activities: lecture / seminar

Number of hours:

per week: 2 / 1 per level/semester: 28 / 14

Form of the course: on-site learning

Wolfgang Kaim, Brigitte Schwederski, Axel Klein: Bioinorganic Chemistry: Inorganic Elements in the Chemistry of Life: An Introduction and Guide. Wiesbaden, Wiley 2013.

Dieter Rehder: Bioinorganic Chemistry. Oxford, Oxford Univ. Press 2014. ISBN: 9780199655199

Nils Metzler-Nolte, Ulrich Schatzschneider: Bioinorganic Chemistry: A Practical Course. Berlin, De Gruyter 2009.

1. Introduction to bioinorganic chemistry: Evolution of life on Earth from the point of view of

inorganic chemistry.

2. General considerations, abundance of elements in Nature and living organisms, consequences of changes in chemical composition of Earth ́s crust at earlier stages of evolution of life.

3. Biological functions of inorganic components in living systems. Coordination of metals to

biological ligands.

4. Oxygen: uptake, transport, and storage.

5. Hemoproteins, peroxidases, catalases.

6. Iron: uptake, transport, and storage. Fe-S centers.

7. Biominerals.

8. Bioinorganic chemistry of copper. Bioinorganic chemistry of zinc. Toxicity of inorganic

compounds.

9. Bioinorganic chemistry of molybdenum, vanadium, tungsten. Polyoxometalates.

10. Bioorganometallic chemistry. Medicinal chemistry and applications of coordination compounds

in bioinorganic chemistry: from cis-platin to anti-HIV drugs and beyond. Artificial metalloenzymes.

11. Nuclear medicine: Radioisotopes and their complexes in diagnostics and therapy.

12. Advanced bioinorganic chemistry: inorganic photosynthesis, protein crystallography,

geobiotechnology and other examples.

The seminars will be focused on discussions to the chosen topic of the seminar thesis (finding

scientific information using databases, analysis and extraction of data, writing the thesis).

The seminars are evaluated during the term in the form of a seminar work. It is possible to get the maximum of 25 points for the thesis that will be aimed at the bioinorganic chemistry of a chosen element or group of elements. The teacher announces the topics for the seminar work at the beginning of the term. The students are required to submit the thesis prior to the end of teaching period of the term.

The final evaluation will be done by a written exam, for which the maximum of 75 points will be available.

Grade scale: A 92-100%, B 84-92 %, C 76-84 %, D 68-76 %, E 60-68 %, Fx less than 60 %.

English

1. Introduction to bioinorganic chemistry: Evolution of life on Earth from the point of view of inorganic chemistry.

2. General considerations, abundance of elements in Nature and living organisms, consequences of changes in chemical composition of Earth´s crust at earlier stages of evolution of life.

3. Biological functions of inorganic components in living systems. Coordination of metals to biological ligands.

4. Oxygen: uptake, transport, and storage.

5. Hemoproteins, peroxidases, catalases.

6. Iron: uptake, transport, and storage. Fe-S centers.

7. Biominerals.

8. Bioinorganic chemistry of copper. Bioinorganic chemistry of zinc. Toxicity of inorganic compounds.

9. Bioinorganic chemistry of molybdenum, vanadium, tungsten. Polyoxometalates.

10. Bioorganometallic chemistry. Medicinal chemistry and applications of coordination compounds in bioinorganic chemistry: from cis-platin to anti-HIV drugs and beyond. Artificial metalloenzymes.

11. Nuclear medicine: Radioisotopes and their complexes in diagnostics and therapy.

12. Advanced bioinorganic chemistry: inorganic photosynthesis, protein crystallography, geobiotechnology and other examples.

The seminars will be focused on discussions to the chosen topic of the seminar thesis (finding scientific information using databases, analysis and extraction of data, writing the thesis).

The aim of the course is to familiarize students with basic concepts of modern bioinorganic chemistry of the elements focused mostly on coordination chemistry of transition metal ions. The subjects of the course are as follows: the roles of inorganic components in biological systems, evolution of life on Earth from the point of view of inorganic chemistry, functions of transition metal ions such as compositional and supportive ones, catalytic functions, capture and storage of important (micro)elements, reactivity of small molecules, toxicity. The aim of the seminars is to familiarize students with writing of a longer scientific text in English focused on the chosen topic according to the students´ interests.

Nelson, D. L. a Cox, M.M. (2017) Lehninger Principles of Biochemistry, W.H. Freeman;

Berg J.M., Tymoczko J.L., Gatto G.J. a Stryer L. (2019) Biochemistry, MacMillan

Instructions for each task (will be provided in advance by the exercise teachers).

Students write (10-point) test each exercise. Students have to write a report from each practical task (5-point). Students must attain at least 3 points from each individual test, turn in all lab reports and have least 50% of total points. They will be evaluated as follows: 92% A, 84% B, 76% C, 68% D, 60% E, Fx-less then 60%.

English

course is available in winter semester only

Introduction, safety in the laboratory.

Calculations in the biochemical laboratory.

Carbohydrates - determination of lactose in milk, hydrolysis of disaccharides and testing of reducing properties, thin layer chromatography of carbohydrates.

Animo acids and protein - determination of isoelectric point of casein, test reactions to amino

acids and proteins, SDS - polyacrylamide gel electrophoresis. Gel filtration of haemoglobin.

Enzymes - determination of kinetic parameters of beta-galactosidase. Determination of pH optimum and temperature optimum of salivary amylase.

Lipids - determination of cholesterol in the egg yolk.

Photosynthesis.

DNA - plasmid DNA isolation. Bacterial transformation.

Amino acid metabolism - determination of urea in serum and urine, determination of creatinine in serum.

During the exercise, students will practically verify some of the knowledge acquired during lectures and seminars in the subject Biochemistry (1) (N–bCXX–000) and get acquainted with basic biochemical methods.

Type of activities: 2 h lecture and 1 h seminar per week, full-time study

Number of hours:

per week: 2/1 per level/semester: 26/13

Form of the course: present

M.B. Smith: Organic Synthesis, McGraw-Hill, Inc., 1994. P.J. Kocieński: Protecting groups,

Thieme Stuttgart, 1994. G. S. Zweifel, M. H. Nantz: Modern Organic Synthesis, W. H.

Freeman, 2006. Paul Wyatt, Stuart Warren: Organic Synthesis: Strategy and Control, Wiley,

2007.

There will be one running written test during the semester and the final

test, each for 100 points. For grade A, it is necessary to obtain at least 92 %, for grade B at

least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 %

of all points from both tests.

English

Introduction of halogen, nitrogen, oxygen and sulfur functional groups into

a molecule.Radical and electrophilic halogenation. Addition to double and triple bonds.

Sulfonation, chlorosulfonation, nitration, nitozation of aliphatic and aromatic compounds.

Hydroboration, epoxidation and dihydroxylation. Vicarial nucleophilic substitution of

aromatic compounds. Ozonolysis and oxidation.

Transformation of halogenoderivatives, alcohols, nitrogen and sulfur compounds.

Nucleophilic substitution, reduction and elimination reactions. Reduction of nitro and

nitrosoderivatives. Preparation and reactions of diazocompounds and diazonium salts.

Syntesis of funcional derivatives of carboxylic acids.

Protecting groups – protection and deprotection, protecting of alcohols, tiols, amines,

carbonyl compounds and carboxylic acids. Protection of reactive positions on benzene ring.

Creation of C-C bonds. Alkylation and acylation of arenes, heteroarenes, alkynes,

enolates and enaminies. Preparation and reactions of organomagnesium, organozinc and

organocopper compounds. Coupling reaction of aromatic compounds. Aldolisation and

relating reactions. Condensation reactions leading to alkenes. Wittig and relating reactions.

Michael additions, Robinson annelation, Mannich reaction. Radical reactions and reactions

of carbenes.

Synthesis of heterocyclic compounds. Nomenclature of heterocycles. 1,3-dipolar

cycloadditions. Paterno-Buchi reaction. Standard synthesis of five-membered heterocyclic

compounds – pyrroles, furanes, thiofenes, indoles, pyrazoles, imidazoles. Synthesis of sixmembered heterocycles – pyridines, pyrylium salts, pyrimidines, quinolines, purines.

This course covers the basic steps of organic synthesis. By the end of this course, students

should be able to:

• Understand and design the methods for the introduction of functional groups into

a molecule, their interconversion and removal.

• Know the properties of majority of protecting groups, their introduction and removal.

• Control the creation of carbon – carbon bonds.

• Design several alternatives for the synthesis of heterocyclic compounds of a specific

type.

Duward Shriver, Peter Atkins: Inorganic Chemistry, 5th edition, 2010, Oxford University Press

Stephen Lower: Chem1 virtual textbook a reference text for General Chemistry

http://www.chem1.com/acad/webtext/virtualtextbook.html

There will be two running written test examinations (maximum 50 points each) during the semester course.

Credits will not be assigned to a student, who will not earn at least 60% from both written tests.

For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % of all points.

English

Nomenclature of inorganic compounds. Chemical reactions, formulae and equations. Structural formulae. Atomic structure; molecular structure. Models of chemical bonding. Hybridization. VSEPR theory. Molecular orbital theory. Bond polarity; electronegativity; oxidation number; ionic bond; hydrogen-bonding; van der Waals interactions. Enthalpy; entropy; laws of thermodynamics; thermochemical laws. Phase – phase transitions. Solid state – structures. The principles of chemical kinetics: reaction rate and order; mechanism; catalysis. Chemical equilibrium. Electrolytic dissociation; Acid-base theories. pH – simple calculations. Hydrolysis. Precipitation reactions. Oxidation and reduction.

Discussion on elements and their basic compounds.

This course covers the topics of the course “General and Inorganic Chemistry” which will be practiced on various examples, exercises and tasks.

Number of contact hours:

per week: 1 /1 per level/semester: 13 / 13

on-site learning, on-line learning

A. Manz, N. Pamme, D. Iossifidi, Bioanalytical Chemistry, Imperial College Press, 2004.

G. Evans (ed.) A Handbook of Bioanalysis and Drug Metabolism, CRC Press 2004.

K. Mitchelson, New High Throughput Technologies for DNA Sequencing and Genomics, Elsevier, 2007.

R. F. Venn, Principles and Practice of Bioanalysis, CRC Press, 2003.

Scientific journals - Analytical and Bioanalytical Chemistry, Journal of Bioanalysis and Biomedicine, Bioseparation, Journal Chromatography B, Journal of Separation Science, Electrophoresis, etc.

Seminar – a maximum of 40 points, for elaboration and presentation of a seminar paper. Lecture – a maximum of 60 points, for the final test. The final grade will consist of evaluation of seminar and the final test from lecture, for a maximum of 100 points. For grade A it is necessary to obtain at least 92 points, for grade B at least 84 points, for grade C at least 76 points, for grade D at least 68 points and for grade E at least 60 points. The evaluation is the same for on-line learning.

English

The course is provided only in the winter semester.The course will switch to distance learning if enrollment falls below 5 students.

• Definition of field of interest, problems, strategies, procedures, methods, applications and the state-of-the-art of bioanalysis in the science system of analytical chemistry.

• Biologically distinct molecules and the need for their determination in biological samples.

• Specific properties and characteristics of biological samples (microbiological, biotechnological, plant, animal, food), sample stability and source of errors, sampling rules, storage, processing, and pretreatment before measurement.

• Clinical samples – blood, serum, plasma, urine, saliva, cerebrospinal fluid, tissues.

• Diagnostic and clinical analysis. Use of biochemical and biological principles for the purpose of chemical analysis of selected substances (e. g., measurement of pH of body fluids, cytometry, cell sorting).

• Specific requirements for bioanalysis instrumentation.

• Solid phase extraction in bioanalysis, biochromatography, denaturing chromatography, electroseparation methods. Specific requirements due to the nature of the biological samples and the limitations of their analysis.

• Bioanalysis in genomics. Relationship between bioseparation methods and PCR.

• Bioanalysis in proteomics. Protein sequencing. Problems of validation in bioanalysis of biomacromolecules.

• Chemical analysis of metabolites - metabolomics, metabolonomics. Criteria for data processing and results interpretation in bioanalysis. Biological samples variability.

• Trends in development of analytical instrumentation and equipment. Biocompatibility of materials used in instrumentation.

Students will get acquainted with the current state of bioanalytical chemistry and with sampling techniques and methods of processing biological samples. The course is also suitable for students of biochemistry or biology who are interested in analytical techniques aimed at investigation of wide range of biomolecules, e.g., hormones, amino acids, peptides, proteins, nucleic acids, carbohydrates, etc. The topic of this course supports interdisciplinary character of bioanalysis through education in electrophoresis, liquid chromatography, biosensors, bioassays, DNA and proteins sequencing, combination of PCR and analytical methods. The content of the objective is complementary to the knowledge that is usually not involved in common textbooks on analytical chemistry. Students will co-solve the problems of case studies in the field of biochemistry, biotechnology, and the other natural sciences.

Type of activities: seminar

Number of hours:

per week: 2 per level/semester: 26

Form of the course: on-site learning / online learning

Nelson, D. L. a Cox, M.M. (2017) Lehninger Principles of Biochemistry, W.H. Freeman;

Berg J.M., Tymoczko J.L., Gatto G.J. a Stryer L. (2019) Biochemistry, MacMillan

During the semester students write 10 tests each by 8 to 15 points. Final grade: 100-90% A, 89-80% B, 79-70% C, 69-65% D, 64-60% E, Fx-less than 60%

English

Taking Biochemistry class is required to sign up for this course.

1. Carbohydrates. Classification, physico-chemical and biological properties of carbohydrates. Stereochemistry: configuration, conformation, enantiomer, epimer, diastereomer, mutarotation, α-, β-anomers. Glycosidic bond. Oligosaccharides and polysaccharides. Structural polysaccharides, storage polysaccharides - bonds, structures.

2. Amino Acids and Proteins. General formula of AA, classification of AA, formulas of AA, optical activity, spectroscopic properties of AA, acid-base properties of AA, zwitterions, amphoteric character of AA, isoelectric point, structure and properties of the peptide bond. Three-dimensional structure of proteins - primary, secondary (α-helix, β-pleated sheet, β-turn), tertiary, quaternary; bonds (interactions) and functional groups implied in these structures. Classification of proteins according to structure and solubility (fibrous, globular, membrane proteins). Biological functions of proteins, native conformation, denaturation, renaturation.

3. Enzymes. Holoenzyme, apoenzyme, cofactor, coenzyme, prosthetic group. Classification of enzymes. Active site, specificity of enzymes. Mechanism of action of enzymes – “lock and key”, “induced fit”. Activation energy, transition state. Enzyme kinetics, Michaelis - Menten equation, parameters KM and Vmax; enzyme inhibition - irreversible, reversible - competitive, uncompetitive, mixed. Regulation of enzyme activity - allosteric modification, covalent

modification, regulatory proteins, proteolytic cleavage (zymogens).

4. Lipids and Membranes. Functions of the lipids. Structure and properties of fatty acids. Storage lipids: triacylglycerols (fats, oils), waxes. Membrane lipids: glycerophospholipids, sphingolipids, sterols. Amphipathic character of some lipids, aggregated forms of lipids - micelles, bilayers. Biological membranes, membrane proteins, fluid mosaic model.

5. Introduction to metabolism. Sources and transformations of energy in the biosphere. Laws of thermodynamics (1st and 2nd). Chemical energy - enthalpy, free (Gibbs) energy, entropy. Endergonic, exergonic reactions. Carriers of chemical energy. ATP – its role and production in the living systems (substrate-level phosphorylation, oxidative phosphorylation, photophosphorylation). Catabolic and anabolic metabolic pathways. Energy relationships between catabolic and anabolic pathways. Oxidation of biomolecules.

6. Metabolism of glucose. Glucose as a source of metabolic energy. Glycolysis - significance, localization, 2 phases of glycolysis, individual reactions, intermediates and enzymes of glycolysis. Fate of pyruvate. Lactic fermentation, alcoholic fermentation. Gluconeogenesis - significance, substrates, three unique gluconeogenetic steps (4 enzymes), localization. Cori cycle, transfer of lactate from muscle to liver, formation of glucose from lactate. Pentose phosphate pathway: significance, formation of NADPH, ribulose-5-phosphate, reactions catalyzed by dehydrogenases, isomerase, epimerase, transaldolases, transketolase.

7. Krebs cycle. Glyoxylate cycle. Formation of acetyl-coenzyme A from pyruvic acid. Krebs cycle as a source of energy and biosynthetic precursors, cellular localization of the cycle. Krebs cycle reactions, individual intermediates and enzymes. Amphibolic character of the citrate cycle, anaplerotic reactions (pyruvate carboxylase). Glyoxylate cycle - importance for plants and bacteria, localization, enzymes.

8. Metabolism of fatty acids. Fatty acids as a source of metabolic energy. Fats digestion - bile acids, lipases, chylomicrons. The fate of fatty acids in muscle and adipose tissue. Release of fatty acids from adipose tissue and their transfer to tissues. β-oxidation of fatty acids - localization in the cell, transfer of fatty acids to mitochondria (carnitine function). b-oxidation reactions, formation of acetyl-coenzyme A. Fate of acetyl-coenzyme A - entry into the citrate cycle. Fatty acid biosynthesis - comparison with β-oxidation, reactions. Sources of NADPH. Transport of fat and cholesterol in humans, roles of lipoproteins.

9. Oxidative phosphorylation. Structure and functions of mitochondria. Composition and function of the respiratory chain, electron transporters - cytochromes, iron-sulfur proteins, ubiquinone, flavoproteins. The source of electrons entering the respiratory chain. Electron transfer in the respiratory chain (complexes I, II, III, IV, cyt c, ubiquinone). Proton gradient. ATP synthesis, ATP-synthase. Chemiosmotic theory. Alternative use of proton gradient - thermogenesis, movement of bacteria, transport of metabolites.

10. Photosynthesis. Structure and function of chloroplasts. Pigments and their role in photosynthesis. Photochemical reaction centers. Electron transfer by photosystems I and II. Non-cyclic and cyclic photophosphorylation. Photolysis of water. Production of NADPH. Synthesis of carbohydrates during photosynthesis. Three stages of CO2 assimilation. Basic reactions and function of Calvin cycle.

11. Degradation of amino acids and urea cycle; metabolism of nucleotides. Deamination, transamination and decarboxlation of amino acids. Amino-transferases. Fate of NH4+ in various organisms. Urea cycle and its interconnection with citric acid cycle. Biosynthesis of ribonucleotides and deoxyribonucleotides de novo and by salvage reactions. Degradation of nucleic acids. Degradation of purine and pyrimidine bases.

12. Nucleotides and Nucleic Acids. Nitrogenous bases found in RNA and DNA. Nucleosides and nucleotides – their structure and components (nucleobases, sugar, phosphoric acid). Structure of deoxyribonucleic acid: (i) primary structure; (ii) secondary structure and its discovery; (iii) ABZ forms of the secondary structure; (iv) another alternative forms of the secondary structure (cruciform, G-quadruplex, Hoogsteen base pairing); (v) tertiary structure (supercoils, topoisomerases). DNA replication enzymes and the rules – semiconservative, bidirectional, semidiscontinuous (Okazaki fragments). DNA denaturation. Chromosome structure in eukaryotes – the nucleosome and nuclear DNA packing levels. DNA/RNA differences. Structure of ribonucleic acid: (i) primary structure; (ii) secondary structure; (iii) tertiary structure. Various forms of RNA serving different functions in cell – mRNA, rRNA, tRNA, snRNA, snoRNA, ncRNA.

13. Transfer of genetic information. Transcription: General features of transcription, prokaryotes and eukaryotes comparison. Transcription in prokaryotes: initiation, elongation, termination. Transcription in eukaryotes: initiation, elongation, termination and introduction to the mRNA processing. Inhibitors of transcription in prokaryotes and eukaryotes. Genetic code and Translation: Structure of tRNA. Function of tRNA in translation. Genetic code, its features (triplet code, continuous, not overlapping, degenerate, unambiguous, universal). Decoding of the standard genetic code. Natural and unnatural variations in the standard genetic code. Loading the tRNAs and aminoacyl-tRNA synthetases. Codon-Anticodon pairing. Ribosome, its structure, prokaryotes and eukaryotes comparison. Translation – protein synthesis mechanism and stages: initiation, elongation, termination. Translation elongation cycle three principal steps: codon-directed binding, peptide bond formation (ribosome is ribozyme), translocation. Molecular mimicry. Inhibitors of protein synthesis.

14. Recombinant DNA, artificial manipulation with Nucleic acids. Cloning of DNA: history, plasmids, restriction enzymes, ligases, linkers and polylinkers, shuttle vectors. Genomic gDNA library and complementary DNA cDNA library. Preparation of gDNA library and cDNA library. Particular DNA segment identification by hybridization – Southern blotting. Colony hybridization. Polymerase chain reaction – PCR cycle stages: heating, cooling, polymerization. DNA primary structure determination – DNA sequencing methods: Sanger method and Maxam-Gilbert chemical cleavage method.

Seminar is focused on discussions on topics covered by the course Biochemistry, in which students are introduced to biochemical processes taking place in living organisms. After completing the course, they will understand chemical structure of biomolecules in relation to their functions, they will comprehend basics of enzyme catalysis and intermediary metabolism.

Form of Study: lecture and practical

Number of contact hours: 4 h of lectures and 5 h of practical

per week: 9 per level/semester: 117

J. McMurry, Organic Chemistry, Cengage Learning, 2009. J. Clayden, N. Greeves, S. Warren, Organic

Chemistry, Oxford University Press, 2012.

Course will be evaluated by a written test (60% value) and evaluation of practicals (40% value). For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % of all points. Credits will not be assigned to a student, who will not earn at least 60% overall from final exam.

english

1. Introduction to organic chemistry (nomenclature of organic compounds, bonding in organic

compounds, basic principles of stereochemistry, electronic effects, acido-basic properties of

organic compounds) 2. Properties and reactivity of major classes of organic compounds • alkanes,

alkenes, alkynes and dienes • aromatic hydrocarbons • organic halogen derivatives • organometallic

compounds • alcohols, tiols and phenols, ethers, epoxides and sulfides • nitrogen containing

compounds – nitrocompounds and amines • carbonyl compounds – aldehydes, ketones, saccharides •

carboxylic acids and their functional derivatives, such as acyl halogenides, esters, amides,

anhydrides • amino acids, peptides, proteins, lipids • heterocyclic compounds, nucleic acids. 3.

Experimental work shall focus on safety in the organic chemistry laboratory, basic operations for

isolation and purification of organic compounds (crystallization, distillation, extraction, adsorption

chromatography - TLC). Simple syntheses of organic compounds will be trained based on functional

group transformations, isolation of organic compounds from natural sources, indentification of

functional groups by chemical analysis and structure determination based on 1H NMR spectra.

This course covers the basics organic chemistry. By the end of this course students should be able

to: • Understand properties of all major classes of organic compounds. • Understand mechanisms of principal organic reactions. • To solve new problems based on knowledge from lecture and training from seminars • To perform fundamental experimental techniques, analyze results, purify and identify compounds

[1] M. Bishop: An Introduction to Chemistry, Chemistry First. ISBN 978-0-9778105-8-1 (online source); Chapter 10: https://preparatorychemistry.com/Bishop_Chemistry_First.htm; [2] E. N. Ramsden: Calculations for A-level Chemistry, Redwood Books, Trowbridge, Wiltshire, 1993, ISBN 0-7487-1594-0

The seminars are evaluated during the term in the form of two written exams. It is possible to get the maximum of 30 points for the first exam and the maximum of 70 points for the second exam.

Grade scale: A 92-100%, B 84-92 %, C 76-84 %, D 68-76 %, E 60-68 %, FX 60 % and less.

English

Physical quantities used in chemical calculations (extensive, intensive). Weight, volume, density, number of particles (moles), mass, molar mass, molar volume. Rounding results of the calculations. Stoichiometry of chemical compounds. Stoichiometry of chemical equations. Calculations according to chemical equations. Determination of the determining reactant and reactant in excess. Calculations using ideal gas laws. Quantities expressing the composition of solutions. Calculations with the weight fraction. Calculations with substance concentration. Mixing and dilution of solutions. Calculations for the preparation of solutions from anhydrous substances and hydrates. Preparation of saturated solutions. Recalculations of different ways for defining the composition of solutions. Combined calculations - calculations according to chemical equations and calculations related to solutions. Combined calculations - calculations related to syntheses.

By completing the course, the student will acquire the necessary knowledge to implement the basic chemical calculations in the field of stoichiometry, solutions, ideal gas and their mutual

· combinations. Upon successful completion of the education process, the student will be able to be prepared independently for the laboratory exercises in inorganic, organic, and physical chemistry, and in subsequent years to understand subjects related to chemical calculations.

Type of activities: practicals

Number of hours:

per week: 8 per level/semester: 88

Form of the course: on-site learning

Lodish,H. et al.(2016), Molecular Cell Biology, 8th edition, W.H Freeman and Company

J.M.Berg et al. (2015), Biochemistry, 8th edition, W.H Freeman and Company

Sambrook, J., Fritsch, E.F. a Maniatis, T. (1989) Molecular cloning: A laboratory manual, Cold

Spring Harbor Laboratory Press

Students, who achieved more then 60% of the total assessment, will be evaluated as follows: ≥90 % A, ≥80 % B, ≥70 % C, ≥ 65% D, ≥ 60% E. Credits will not be awarded to a student who receives less than 60% of the total assessment (control test and activity during the semester). Students write a 10-point test each exercise. At the end of the semester, students take a final control test, from which they must attain at least 50 %. Scale of assessment (preliminary/final): 60/100 ongoing evaluation/ 40/100 final test (60% ongoing evaluation /40% final test).

English

course is available in summer semester only

Advanced Practice in Biochemistry is a set of modern laboratory methods in biochemistry,

molecular and cell biology. This course will enable students to acquire skills in following techniques:

1. Isolation and restriction analysis of yeast mitochondrial DNA.

2. Egg-white lysozyme purification using ion-exchange chromatography.

3. Yeast Saccharomyces cerevisiae use for transcription studies.

4. Yeast Saccharomyces cerevisiae lipid extraction and separation.

5. Specific antibody determination using ELISA.

Students acquire advanced laboratory skills in biochemical, molecular biological and microbiological techniques. After completing this course students should be able to apply in biochemical and biomedical research.

Number of contact hours:

per week: 4 / 5 per level/semester: 56 / 70

on-site learning

D.A. Skoog, F.J. West, F.J. Holler, S.R. Crouch: Analytical Chemistry. An Introduction, Saunders Coll. Publ., 2000.

G. Schwedt: The Essential Guide to Analytical Chemistry, Wiley, New York, 1997.

R. Kellner, J.M. Mermet, M. Otto, Analytical Chemistry, John Wiley & Sons Australia, 2013.

For practicals: study material available at www.analytika.sk

Lecture – a maximum of 50 points, for the final test. Practicals – a maximum of 50 points, for theoretical preparation for practicals, active participation in practicals, lab reports from practicals and final test from practicals. The final grade will consist of evaluation of the practicals and the final test from lecture, for a maximum of 100 points. For grade A it is necessary to obtain at least 92 points, for grade B at least 84 points, for grade C at least 76 points, for grade D at least 68 points and for grade E at least 60 points. The evaluation is the same for on-line learning.

English

The course is provided only in the summer semester.

• Definition, subject of interest and resources of analytical chemistry.

• Relationship between analytical chemistry and chemical analysis. Analytical method (classification). Analytical principle. Sampling.

• Measurement (qualitative and quantitative analysis). Analytical signal and its properties. Calibration. Statistical evaluation of data (measurement errors).

• Simple sample preparation procedures. Decomposition of inorganic and organic samples, extraction.

• Chemical methods of analysis (qualitative, quantitative). Evidence of chemical reactions and tests, gravimetric analysis, volumetric analysis. Titration curves. Principles of neutralization, precipitation, redox and complexometric titrations.

• Chemical equilibria (acid-base, complex-forming, precipitating, redox).

• Electroanalytical methods. Basic scheme of electrochemical cell. Classification of electroanalytical methods. Equilibrium potentiometry (reference and indicator electrodes, direct potentiometry and potentiometric titrations, ion-selective electrodes as a selectivity coefficient). Principle and use of linear and cyclic voltammetry, coulometry and conductometry.

• Optical analytical methods. Properties of electromagnetic radiation. History and classification of optical methods. Basic instrumentation of optical analytical methods. Atomic spectrometry. Atomic spectrometry techniques.

• Molecular spectrometry. Molecular spectrometry techniques – absorption UV-VIS spectrophotometry, spectrofluorometry, infrared and Raman spectrometry. Non-spectral optical methods. Reflectometry, interferometry, polarimetry, turbidimetry and nephelometry.

• Mass spectrometry. Basic principles. Basic scheme of equipment. Measurement conditions. Instrumentation in mass spectrometry. Basic types of ionization techniques and ion sources.

• Separation techniques, their function and importance in analytical procedures. Classification of separation principles and methods. Precipitation and filtration. Separation of volatile substances by distillation. Isolation and separation of substances by extraction. Ion-exchange. Chromatographic separation. Classification of chromatographic methods. Gas chromatography – principles and instrumentation. High-performance liquid chromatography – principle and instrumentation. Electroseparation methods. Capillary electrophoresis vs planar techniques. Instrumentation. Basic principles of electrophoretic methods: zone electrophoresis, isotachophoresis, isoelectric focusing.

• Automation in analytical laboratories. The application of combined analytical methods to solve selected analytical problems.

Practicals

• Volumetric analysis. Determination of calcium and magnesium in water.

• Potentiometric analysis. Determination of acetic acid in fermented spirit vinegar.

• Optical analytical methods. Determination of calcium and sodium in mineral water by emission flame photometry. Spectrophotometric determination of copper in the water. Identification and quantification of synthetic dyes by molecular absorption spectrometry.

• Chromatographic separation methods. Determination of methanol in alcoholic beverages by GC. RP-HPLC separation of aromatic hydroxycompounds and gallic acid. Separation of water-soluble dyes by paper chromatography.

• Electroseparation methods. Isotachophoretic separation of synthetic dyes using column-coupling technique. Isotachophoretic determination of glutamate in food.

Students will get acquainted with the current state of quantitative observation; generation of analytical signal; analytical processes, principles, procedures and techniques and their classification; solving identification problems; and characterization and quantification of chemical substances in science and technology. Students will also get acquainted with the possibility of detecting and finding solutions to materials research, production and social practice using chemical analysis as a tool of analytical chemistry. Students will also get acquainted with instrumental experimental work in the laboratory.

Form of Study: lecture / seminar

Number of contact hours:

per week: 2 / 1 per level/semester: 26 / 13

J. Clayden, N. Greeves and S. Warren, Organic Chemistry, Oxford University Press, 2012.

Grades will be based on the results of seminar (activity and accomplishment of homeworks, weight 0.2), two written tests focused on understanding of mechanisms of organic reactions (weights 0.2 and 0.4) and oral exam (weight 0.2). More than 50% of points must be obtained from each part of the grading. The course has a standardized grading system which is identified below:

A (92 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of

original thinking and obvious capacity to analyze, synthesize and evaluate. B (84 – 91 %): Good,

competent work; laudable performance with evidence of some original thinking, good problemsolving ability, exhibiting a serious, responsible engagement with the course content.C (76 – 83 %): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (68 – 75 %). Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 67 %): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

english

offered in summer semester only

1) Introduction to the intermediate level of organic chemistry. Advanced understanding of bonding

in organic compounds, delocalization and conjugation, electronic effects, orbital approach. Kinetics

and thermodynamics of organic reactions.

2) Mechanisms of basic kinds of organic reactions. Electrophilic additions and substitutions.

Nucleophilic substitutions and eliminations at saturated carbon, nucleophilic aromatic

substitutions. Nucleophilic additions at carbonyl carbon. Reactions of enolates and conjugated

additions. Radical reactions.

3) Selected modern methods in organic synthesis. Organometallic compounds and their applications in C–C bond formation. Chemoselectivity and regioselectivity, protection and transformation of functional groups.

This course provides overview of organic chemistry from the mechanistic point of view, based on

advanced bonding theory. It covers also bifunctional derivatives, effect of reaction conditions, etc.

Modern synthetic methods are also included.

By the end of this course students should be able to:

• Articulate a have general understanding of reaction mechanisms in organic chemistry,

based on chemical structure, bonding, reaction conditions, etc.

• Propose synthetic approaches, describe detailed mechanism of the reaction with

explanation of steric and electronic effects.

Form of Study: seminar / laboratory exercises

Number of contact hours:

per week: 3 per semester: 39

L. M. Harwood, C. J. Moody, J. M. Percy, Experimental Organic Chemistry: Standard and Microscale,

Wiley, 1998.

Grades will be based on the results of practical work (weight 0.2 per each of three experiments) and final test (weight 0.4). Evaluation of each experiment consists of technique (50%), product yield and purity (25%) and protocol (25%). The course has a system which is identified below:

A (92 – 100%), B (84 – 91 %), C (76 – 83 %), D (68 – 75 %), E (60 – 67 %), Fx (under 60 %).

english

offered in summer semester only, it is taught as a block at the end of the semester: 2h introductory seminar, 3 x 10-12h exercises, 2h final test

1) Laboratory safety, theory of advanced laboratory techniques.

2) Synthesis of diethyl oxalate (diethyl succinate) – application of azeotropic distillation for water

removal from the reaction mixture, purification of the product by distillation under reduced

pressure, confirmation of the product identity by refractive index.

3) Preparation of triphenylmethanol – reaction under inert conditions, removal of constituents by

steam distillation, purification of the product by crystallization, confirmation of the product

identity by melting point.

4) Acylation of ferrocene with acetyl chloride – thin layer and preparative column chromatography,

product identification (TLC, melting point).

This course is aimed to gain practical skills in advanced reaction and separation laboratory

techniques, such as synthesis under inert reaction conditions, separation of the product by various

distillation techniques (distillation under reduced pressure, fraction distillation, steam

distillation), and preparative column chromatography.

By the end of this course students should be able to understand the skills, knowledge, and

experience needed for organic synthesis and preparative separation of organic compounds.

Specifically, as recommended by supervisor

Grades will be based on the final practical training report (contributing 100%), which has a standardized grading system identified below: A (91 – 100%): Outstanding, excellent work (exceptional performance with strong evidence of original thinking and obvious capacity to analyze, synthesize and evaluate. B (81 – 90 %): Good, competent work; laudable performance with evidence of some original thinking, good problem-solving ability, exhibiting a serious, responsible engagement with the course content. C (73 – 80%): Adequate, reasonably satisfactory work; fair performance but infrequent evidence of original thinking or the capacity to analyze, satisfies the minimum requirements of the course. D (66 – 72%): Less acceptable work; relatively weak performance with little evidence of original thinking or ability to analyze or synthesize course material. E (60 – 65%): Minimally acceptable work; very weak performance with little evidence of original thinking, showing inadequate grasp of some basic elements of the course. Fx (under 60%): Inadequate work; poor performance that indicates a lack of understanding or misunderstanding of essential subject matter.

English

The course can be completed only after the exams in the summer semester.

The course represents three weeks of practical work after passing the exams in the summer semester. Students participating in the course of real research conducted in laboratories of Comenius University, Slovak Academy of Sciences and private research institutions led by experts working in the biological or chemical fields.

During practice, students will improve their skill in laboratory techniques and expand their theoretical knowledge in the study area and enables close collaboration with professional research groups.

Number of contact hours:

per week: 2 per level/semester: 26

on-site learning

D.A. Skoog, F.J. West, F.J. Holler, S.R. Crouch: Analytical Chemistry. An Introduction, Saunders Coll. Publ., 2000.

Current monographic and original article literature and information sources on the Internet.

Original and review articles in scientific journals.

Seminar – a maximum of 100 points, for active participation in seminars - a maximum of 30 points, for elaboration and presentation of a seminar paper – a maximum of 70 points. For grade A it is necessary to obtain at least 92 points, for grade B at least 84 points, for grade C at least 76 points, for grade D at least 68 points and for grade E at least 60 points.

English

The course is provided only in the summer semester. If less than 3 students enroll, the course will be provided in individual form.

• History of analytical chemistry in the context of the development of society.

• Methodology of analytical procedure.

• Working characteristics of the analytical methods. Calculation of measurement errors.

• Examples of the use of sample preparation procedures in chemical analysis.

• Analytical use of neutralization, precipitation, redox and complexometric titrations.

• Chemical stoichiometry.

• Analytical applications of equilibrium potentiometry, voltammetry, coulometry and conductometry.

• Analytical applications of atomic spectrometry methods.

• Analytical applications of molecular spectrometry and non-spectral optical methods.

• Analytical applications of mass spectrometry.

• Application of separation methods in chemical analysis.

• The combined application of analytical methods to solve selected analytical problems.

• Practical examples of the use of analytical techniques in chemical analysis procedures in solving current practical problems.

Individual topics of seminar work will include examples of practical use of analytical techniques mentioned above in food, environmental and pharmaceutical analysis and bioanalysis.

The objective involves calculations in analytical chemistry and solution of model situations from social practice, which are discussed in daily press and information media. Students will solve case studies from biochemistry, biotechnology, and other natural sciences. The current use of analytical chemistry methods and their future potential and an outline of their development trends will be discussed. Students will get acquainted with the possibility of analysis of biomedical, environmental, food and pharmaceutical samples.

Form of Study: seminar

Number of contact hours: 2 h of seminars

per week: 2 per level/semester: 26

J. McMurry, Organic Chemistry, Cengage Learning, 2009. J. Clayden, N. Greeves, S. Warren, Organic

Chemistry, Oxford University Press, 2012.

Course will be evaluated by a written test. For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % of all points. Credits will not be assigned to a student, who will not earn at least 60% of points in the test.

english

Introduction to organic chemistry - nomenclature of organic compounds, bonding in organic

compounds, basic principles of stereochemistry, electronic effects, acido-basic properties of

organic compounds). Properties and and typical reactions (both syntheses of specific compounds as

well as their reactions) of major classes of organic compounds: alkanes, alkenes, alkynes and

dienes; aromatic hydrocarbons; organic halogen derivatives; organometallic compounds; alcohols,

tiols and phenols, ethers, epoxides and sulfides; nitrogen containing compounds – nitrocompounds

and amines; carbonyl compounds – aldehydes, ketones, saccharides; carboxylic acids and their

functional derivatives, such as acyl halogenides, esters, amides, anhydrides; amino acids, peptides,

proteins, lipids; heterocyclic compounds, nucleic acids. Basics of multistep organic synthesis will

practiced on seminars too. Attention will be also devoted to basic applications of spectroscopy

techniques, mainly 1H NMR.

This course aims to improve understanding of basics organic chemistry via individual students work

on the seminars, were assignements on topic from the organic chemistry lecture will be discussed.

By the end of this course students should be able to understand properties of all major classes of

organic compounds, understand mechanisms of typical organic reactions, to solve new problems

based on knowledge from lecture and training from seminars.

•Walter D. Loveland, David J. Morrissey, Glenn T. Seaborg (2006). Modern Nuclear Chemistry. John Wiley & Sons, Inc. ISBN:9780471115328. •József Kónya, Noémi M. Nagy (2012). Nuclear and Radiochemistry. ELSEVIER. ISBN 978-0-12-391430-9. DOI https://doi.org/10.1016/C2011-0-06943-0 •Gregory Choppin (2013) Radiochemistry and Nuclear Chemistry. Elsevier Books. EAN: 9780124058972.

The applicant successful graduation of the course is to obtain minimally 60 % of points of the final examination: seminar work (50%) + examination (50%). For the grade A (excellent) it is necessary to obtain at least 92–100%, to obtain the grade B (very good) at least 84–91%, for the grade C (good) at least 76–83%, for the grade D (satisfactory) at least 68– 75% and for E rating (adequate) at least 60–67%. A rating below 60% is rated as FX (insufficient).

1.-2. Nuclear chemistry fundamentals: nuclear decay, nuclear properties, and kinetics of nuclear decay. 3. Interaction with matter. 4.-5. Production of radionuclides. 6. Nuclear reactions and nuclear fission. 7. Nuclear Analytical Techniques. 8. Detection of radiation and measurement techniques. 9. Radiation therapy. 10. Radiotracers. 11. Radiochemical separation techniques. 12.-13. Nuclear energy – nuclear power plants, nuclear fuel cycle, nuclear wastes.

Radiochemistry or nuclear chemistry is the study of radiation from an atomic and molecular perspective, including elemental transformation and reaction effects, as well as physical, health and medical properties. Based on this students how to use radioactivity as a tool for chemically related research and related fields (for example material science, biochemistry, and medicine). The course teaches students fundamental radiochemical methods for qualitative and quantitative analysis of radionuclides in various media. The principles for the detection of radioactive radiation and material will be thoroughly covered.

Form of Study: seminar

Number of contact hours: 2 h of seminars

per week: 2 per level/semester: 26

J. McMurry, Organic Chemistry, Cengage Learning, 2009. J. Clayden, N. Greeves, S. Warren, Organic

Chemistry, Oxford University Press, 2012.

Course will be evaluated by a written test. For grade A, it is necessary to obtain at least 92 %, for grade B at least 84 %, for grade C at least 76 %, for grade D at least 68 % and for grade E at least 60 % of all points. Credits will not be assigned to a student, who will not earn at least 60% of points in the test.

english

Introduction to organic chemistry - nomenclature of organic compounds, bonding in organic

compounds, basic principles of stereochemistry, electronic effects, acido-basic properties of

organic compounds). Properties and and typical reactions (both syntheses of specific compounds as

well as their reactions) of major classes of organic compounds: alkanes, alkenes, alkynes and

dienes; aromatic hydrocarbons; organic halogen derivatives; organometallic compounds; alcohols,

tiols and phenols, ethers, epoxides and sulfides; nitrogen containing compounds – nitrocompounds

and amines; carbonyl compounds – aldehydes, ketones, saccharides; carboxylic acids and their

functional derivatives, such as acyl halogenides, esters, amides, anhydrides; amino acids, peptides,

proteins, lipids; heterocyclic compounds, nucleic acids. Basics of multistep organic synthesis will

practiced on seminars too. Attention will be also devoted to basic applications of spectroscopy

techniques, mainly 1H NMR.

This course aims to streghthen understanding of basics concepts in organic chemistry via individual

students work on the seminars, were assignements on topic from the organic chemistry lecture will

be discussed. This seminar aims to provide additional training in core organic chemistry topics and

thus help understand important concepts from lecture Organic Chemistry. By the end of this course

students should be able to understand basic properties of common organic compounds, understand mechanisms of typical organic reactions.

•Podgorsak E.B.: Radiation Oncology Physics: A Handbook for Teachers and Students. Vienna, IAEA Publication, 2005. ISBN: 92-0-107304-6. •Pöschl, M., Nollet, L.: Radionuclide Concentrations in Food and the Environment. Boca Raton - London - New York : CRC Press, Taylor & Francis Group, 2007. ISBN 0-8493-3594-9. •Bailey D.L., Humm J.L., Todd-Pokropek A., van Aswegen A.: Radiation Medicine Physics: A Handbook for Teachers and Students. Vienna, IAEA Publication, 2014. ISBN: 978-92-0-143810-2.

The applicant successful graduation of the course is to obtain minimally 50 % of points of the final examination: seminar work (50%) + examination (50%). For the grade A (excellent) it is necessary to obtain at least 92–100%, to obtain the grade B (very good) at least 84–91%, for the grade C (good) at least 76–83%, for the grade D (satisfactory) at least 68– 75% and for E rating (adequate) at least 60–67%. A rating below 60% is rated as FX (insufficient).

1. The subject and historical overview of radiobiology, radiation sensitivity of biological species. 2. Physical basics of radiobiology, quantities and terminology. 3. DNA- and cell damage produced by ionizing radiation, biological effect vs. dose curves. 4. Modification of cell damage by radiation, radioprotectors and radiation sensitivity. 5. Repair of cell damage induced by radiation. 6. Molecular radiation biology and biochemistry, the effect of ionizing radiation on metabolism. 7. Radiation syndroms (sickness) and their modulation: bone marrow syndrom, gastrointestinal syndrom, central nervous system syndrom. 8. Radiation sicknesses: acute and chronic cases, their classification, development, diagnosis, therapy. 9. Radiation induced tissue damage, radiation effect on embryo and fetus. 10. Radiation application and incorporated radionuclides in medicíne. Radiotherapy - external and internal. 11. Theoretical conception of mechanisms involved in ionizing radiation systemic effects. 12. After-effects of ionizing radiation: somatic and genetic, limit doses, ALARA, radiation-induced cancer, risk factors, dose response.

Course covers the physical and chemical basics of radiobiology, cell- organism interaction with radiation and radiation damage repair, the applications of ionizing and non-ionizing radiation in medicine. Within the frame of the course is the visit of workplace focused on radiobiology. Students who enroll in this course can benefit from the following: physical basics of radiobiology, mechanisms of effects of ionizing radiation on living organisms and cell repair mechanisms, radiation-caused diseases and therapy, radiation syndromes, protection of the organisms against radiation damage, the usage of ionizing and non-ionizing radiation in medicine, the effects of solar UV radiation and protection.

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Course will be evaluated by a written test in the exam period. For the grade A (excellent) it is necessary to obtain at least 92–100%, to obtain the grade B (very good) at least 84–91%, for the grade C (good) at least 76–83%, for the grade D (satisfactory) at least 68– 75% and for E rating (adequate) at least 60–67%. A rating below 60% is rated as FX (insufficient).

English

· European legislation and international standards.

· Chemical safety and biosafety – chemical safety assessment, EU laws on chemicals (REACH and CLP regulations), chemical safety cards, the Cartagena Protocol on biosafety

· Intellectual property rights in life sciences.

· Toxicology – routes of entry of chemicals into the body, mechanism of action of toxic and very toxic substances on the body, the causes and symptoms of poisoning, biotransformation and excretion from the body

· Basic rules for working with genetically modified organisms (GMO). Requirements for equipment to work with GMOs I. and II. category

· Ethical issues in genetics.

· Radiation and safety – sources of radiation, biological effects of ionizing radiation, principles of radiation protection, application of the basic safety standards

· Principles of good practice (GLP) – definitions of terms, Quality Assurance and GLP, Compliance of Laboratory Suppliers with GLP principles, the application of the GLP principles to non-clinical studies

· Application of radioisotopes in biology, biochemistry and medicine

· Threat of terrorism – chemical, biological and nuclear weapons

Students become aware of legislative and normative aspects of chemistry with emphases of European legislation and international standards. After completing of course, they should know the legal regulations concerning the handling of hazardous chemicals, health and environmental risks of toxic and radioactive substances, genetically modified organisms. They should know the quality management systems of laboratory activities, systems assurance and quality control of chemicals, pharmaceuticals, and food.