The aim of the course is to introduce students to basic concepts of chemical structure and the role of biologically important compounds, as well as the study of kinetics, energy and equilibrium processes important for the normal functioning of living cells.
Chemistry in Medicine, being a part of Medical Biochemistry and Chemistry Course, is taught for 9 weeks and precedes Biochemistry Course. The course is so organized as to deal with relevant topics in Chemistry (General, Inorganic, Organic and Chemistry of Natural Products) and explain chemical concepts essential for the understanding and study of complex problems of Medical Biochemistry.
Informator: MEDICAL BIOCHEMISTRY AND CHEMISTRY
Professors:
- Prof. Kristina Gopčević, PhD
- Prof. Danijela Krstić, PhD
- Assoc. Prof. Nataša Avramović, PhD
- Assoc. Prof. Lidija Izrael Živković, PhD
- Assist. Prof. Ana Medić, PhD
Associates:
- Asst. Teodora Djukić
- Asst. Zorana Lopandić
Course Director: Prof. Kristina Gopčević, PhD
Chemistry in Medicine represents a part of the Medical Biochemistry Course in the second year of integrated studies of medicine and is taught in the first nine weeks in III semester.
The total number of classes of all instruction forms is 72, that is, 8 classes per week (3 classes of lecture, 2 classes of seminars, and 3 classes of practicals) during the 9 weeks of the winter semester.
CHEMISTRY IN MEDICINE
Curriculum
2024/2025 academic year
(III semester)
Week I
Lecture and Seminar
Chemical bonds. Water and water solutions.
Chemical bonds - ionic bond, nonpolar and polar covalent bond; coordinate covalent bond.
Structure, chemical and physical properties of water. Water as a universal solvent. Influence of chemical structure on solubility (polar, nonpolar, amphipathic molecules) and principles of dissolution. Intermolecular interactions (hydrogen bonding, hydrophobic effect). The influence of water on structure of biomacromolecules.
Characteristics of solutions (physiological solutions).
Dissolution of gases in water, Henry's Law (decompression sickness, inhalation anesthesia).
The concept of osmol and solution osmolality; difference in osmolality between electrolyte solution and nonelectrolyte solution with same concentrations.
Colloidal solutions-properties. Colloidal solutions of biomacromolecules (solutions of proteins, nucleic acids). Stability of colloidal solution. Principles of dialysis, hemodialysis.
Lab
Solutions, quantitive composition of solutions
a) Preparing a solution of a particular concentration starting from a solid substance - calculating required mass measuring on a digital scale, dissolution, and quantitative transfer of substances in a volumetric flask.
b) Preparing a solution of desired concentration by diluting concentrated solution - calculating necessary volume, the use of automatic pipettes, and proper use of volumetric flasks.
Preparing serial dilution of solutions (twofold and tenfold).
Week II
Lecture and Seminar
Thermodynamics of living systems. Chemical equilibrium.
Thermodynamics of living systems
Repetitorium: Basic thermodynamic functions: enthalpy, entropy, and Gibbs free energy.
Free energy is an indicator of spontaneity in biochemical reactions. Exergonic and endergonic reactions. Standard free energy and equilibrium constant in biochemical reactions.
Connecting endergonic and exergonic reactions as a thermodynamic basis for the functioning of metabolism. Energy-rich bonds. The role of ATP in energy-coupled reactions.
Chemical equilibrium
Repetitorium: The rate of chemical reaction, activation energy, transition state theory; Factors affecting the rate of chemical reactions (nature of substance, concentration, pressure in gaseous systems, temperature, radiation, catalysts (homogeneous and heterogeneous catalysis)).
Molecularity and order of chemical reaction; elementary and complex chemical reactions. Determination of the activation energy.
Chemical equilibrium in homogeneous and heterogeneous systems. The equilibrium constant. Shifting equilibrium: Le Chatelier's principle. Strong and weak electrolytes.
Lab
Determination of activation energy for hydrolysis reaction of sucrose in an acidic medium.
Optical methods. Application of Lambert-Beer's Law, the principle of colorimetry and spectrophotometry. Making a calibration curve with a series of standard solutions (solution of reducing sugars, i.e. glucose and fructose).
Performing reactions of hydrolysis of sucrose in the presence of HCl at two different temperatures.
Calculation: concentrations of reducing sugars by the line equation of a standard curve, the rate of sucrose hydrolysis, the rate constant of sucrose hydrolysis, logarithm of the rate constant of sucrose hydrolysis, and activation energy.
Week III
Lecture and Seminar
Acid-base equilibrium. Buffers.
Repetitorium: Theories of acids and bases. Dissociation of acids and bases. Amphoteric electrolytes. Ionic product of water, pH. Neutralization. Hydrolysis of salts. Solubility product constant.
The concentration of H+ ions and pH of body fluids.
Buffers
Regulation of hydrogen H+ ion concentration in human body fluids, the role of chemical buffers. Henderson-Hasselbach equation. Buffering capacity. Buffers systems in the blood. (Bicarbonate, Posphate and Protein buffer); Ammonia buffer.
Lab
Buffers
Preparing of buffer solution and measuring of pH value on pH-meter.
Demonstration of using software packages available on the Internet so-called „Buffer calculator" for preparation of important biochemical buffer solutions (Tris-HCl, amino acid buffers, carboxylic acid buffers).
Week IV
Lecture and Seminar
Reactivity of biologically important functional groups
Repetitorium: Organic carbon compounds. Nature and polarity of chemical bonds in organic molecules. Isomerism. Electronic effects in organic molecules. Types of reactions in organic chemistry. Aromatic compounds, properties, and reactivity. Heterocyclic compounds.
Double bond- Structure, cis-trans isomerism, and reactivity of unsaturated compounds; addition of water to the double bond in physiological conditions (such as hydration of fumarate to malate in the presence of fumarate hydratase);
Conjugated diene-isoprene and its biologically important derivatives with polyene structure: retinol (vitamin A), and tocopherol (vitamin E).
Heterocyclic compounds and their derivatives in biological structures
A five-membered and six-member heterocyclic compounds having one to two heteroatoms:
-Pyrrole derivatives-heme and porphyrin structures and their importance in the transfer of oxygen in the blood.
-Furan and pyran derivatives in cyclic forms of monosaccharides.
-Thiophene and its derivative biotin (vitamin H).
-Imidazole and its derivatives histidine and histamine.
-Pyridine and its derivatives- nicotinic acid and nicotinamide as reactive part of coenzymes NAD+ and NADP.
-Pyrimidine and its derivatives-pyrimidine bases (cytosine, uracil, thymine).
Compounds with condensed heterocyclic rings:
-Purine and its derivatives-purine bases (adenine, guanine)
Lab
Quantitive determination of electrolytes
Biologically important ions, importance of Na+, K+, Mg2+, Ca2+, Cl-, HCO3- and phosphates in organism.
The principle of volumetry. Volumetric determination of electrolytes in serum.
a) Determination of concentration of Cl- ions in solution by Mohr's method.
b) Determination of concentration of bicarbonate ion in solution by retitration with NaOH standard solution.
Complex compounds, structure, and importance in medicine (EDTA, cis-Pt).
c) Complexometric determination of Ca2+ ion concentration in solution using a standard solution of complexon III.
Week V
Lecture and Seminar
Hydroxyl group, Thiol/Mercapto group, Amino group, Carbonyl group
1) Hydroxyl -OH group
Repetitorium: nomenclature, classification, and solubility of alcohols and phenols.
-Reactions:
1. Oxidation of -OH group to a carbonyl C=O group.
Principles of oxido-reduction in organic chemistry vs. oxido-reduction principles in physiological conditions: oxidation of ethanol by alcohol dehydrogenase in the presence of NAD+.
2. Dehydration and formation of a double C=C bond.
-OH group as a reactive part of the malic acid and the physiologically important reaction of dehydration of malate to fumarate.
3. Esterification of -OH group.
Esters with organic and inorganic acids (phosphoric and nitric acids), pharmacological significance of glycerol trinitrate, and esters of phosphoric acid.
Biologically important derivatives of dihydroxy phenols: hydroquinone/ quinone, and coenzyme Q.
2) Thiol/Mercapto -SH group
Reactivity of thiol/mercapto/sulfhydryl group in biomolecules (oxidation to disulfide; formation of thioesters with acids, formation of insoluble salts with heavy metals - toxicity of heavy metals based on denaturation of proteins).
Metabolically important thiols and their derivatives cysteine, cystine as a product of oxidation of cysteine; methionine as a thioether; and acetyl-CoA as a thioester (importance in transfer of acetyl group).
3) Amino -NH2 group
Repetitorium: structure and reactivity of amines: basicity, alkylation, acylation.
Biologically important amines (catecholamines: adrenaline, noradrenaline, dopamine); diamines (putrescine, cadaverine) and amine derivatives: sulfanilic acid and sulfanilamide (inhibition of synthesis of folate by sulphanilamide).
4) Carbonyl -C=O group
Repetitorium: classification and nomenclature of carbonyl compounds.
Biologically important reactions of nucleophilic addition to carbonyl group:
1. Reduction of carbonyl compounds to alcohols; reduction with NADH.
2. Formation of hemiacetals and acetals; Cyclic hemiacetals as forms of monosaccharides in water solutions.
3. Addition of ammonia and amines to carbonyl compounds (imine formation- Schiff's bases).
4. Aldol-addition reactions.
Lab
Reactions of biologically important functional groups
Reactivity of -OH group in alcohols and phenols: oxidation of ethanol to acetic acid, esterification of ethanol and benzoic acid, formation of colored complex of phenol with iron(III) chloride.
Reactivity of >C=O group: Frommer's reaction with acetone, oxidation of aldehyde with mild oxidizing agent, reactivity of alpha-hydrogen atoms of aldehyde/ketone (iodoformic reaction).
Reactivity of -COOH group: Oxidation of lactic acid, decarboxylation of pyruvic acid, reaction of lactic acid with FeCl3.
Reactions of amides of acids: decomposition of urea in the presence of enzyme urease.
Week VI
Lecture and Seminar
Carboxyl -COOH group, Substituted carboxylic acids (hydroxy, oxo); Anhydrides, Esters, Amides; Biological redox reactions
1) Carboxyl -COOH group
Repetitorium: homologous sequences of saturated and unsaturated, mono and dicarboxylic acids, formulas and names. Reactivity of -COOH group.
Biologically important carboxylic acid such as metabolites of citric acid cycle (malic, succinic, glutaric and fumaric acid); succinate oxidation to fumarate; oxidation of succinate in physiological conditions in the presence of succinate dehydrogenase and FAD as a coenzyme.
2. Substituted carboxylic acids (hydroxy, oxo):
1) Structure and stereochemistry of physiologically important hydroxy carboxylic acids (lactic, malic, citric), pharmacologically important hydroxy carboxylic acids (mandelic, tropic, salicylic) and their derivatives (aspirin, salol).
Oxidation reactions of hydroxy carboxylic acids to oxo carboxylic acids, dehydration reactions to unsaturated acids (malic acid to fumaric acid) or to lactones (ascorbic acid)
2) Reactions of oxo carboxylic acids (pyruvic, oxaloacetic, a-ketoglutaric, acetoacetic) in physiological conditions:
-Reduction of pyruvate to lactate by lactate dehydrogenase in the presence of NADH.
-Aldol addition of oxaloacetate and acetyl-CoA and formation of citric acid.
-Obtaining ketone bodies: b-hydroxy butyric acid, acetoacetic acid and acetone; reduction of acetoacetate to b-hydroxy butyric acid; non-enzymatic decarboxylation of acetoacetate.
3. Anhydrides, esters, amides
1) Biologically important anhydrides:
Phosphoanhydride bonds in ATP and its hydrolysis with energy release; formation of anhydride bond in reaction of fatty acid activation with ATP in the presence of enzyme;
2) Biologically important esters:
-Thioestar bond in acetyl-CoA, hydrolysis of thioestar bond and release of acetyl group;
-Cyclic esters- lactones (Vitamin C); macrolactones (macrolide antibiotics)
3) Biologically important amides:
-Amide bond in biogenic amides (asparagine and glutamine); pharmacologically important amides (phenacetin, paracetamol);
-Cyclic amides-lactams (b-lactam antibiotics: penicillins and cephalosporins)
-Diamide of carbonic acid-urea; urea derivatives.
4. Biological redox reactions
Standard and biological redox potentials. Relationship between standard free energy change and redox potential, prediction of spontaneous chemical reaction.
Important biological redox systems: (NAD+/NADH; glutathione(ox)/glutathione(red); pyruvate/lactate; dehydroascorbate/ascorbate).
Electrochemical potentials of biological redox couples and gradual transfer of electrons through biological redox systems. Transfer of electrons from NADH to O2 in mitochondria in oxidative phosphorylation.
Free radicals: reactive species of oxygen and nitrogen, mechanism of their formation, physiological role. Antioxidants: enzymatic and non-enzymatic. Oxidative stress and consequences of free radical action with intracellular molecules: lipids, proteins, DNA.
Lab
Redox reactions of organic compounds and biomolecules
Oxidation of double bond in natural products.
Oxidation of -OH group (primary and secondary) in alcohols; Oxalic acid oxidation.
Biological redox systems: vitamin C, glutathione.
Reactive oxygen species (hydrogen peroxide).
Colloidal solutions of biomacromolecules.
Dialysis of proteins. Determination of isoelectric point of casein.
Week VII
Lecture and Seminar
Amino acids, Peptides, Proteins
Amino acids
Structures and stereochemistry of amino acids. Proteinogenic amino acids in physiological conditions-zwitter ions. Amphoteric and buffer properties of amino acids.
-Reactivity of amino acids:
-Reaction of -COOH group (decarboxylation and amine formation);
-Reaction of -NH2 group (transamination and ketocarboxylic acids formation);
-Side chain reactions as basis for understanding the most common post-translational modifications (phosphorylation of Ser, Thr, Tyr; N-glycosylation of Asn).
Petides
Formation and properties of peptide bond. Amino acids sequence in peptides. Glutathione and its role in oxidative stress. Structure and physiological role of peptide hormones (bradykinin, oxytocin, vasopressin, insulin). Structure and pharmacological activity of opioid peptides (Met-enkephalin, Leu-enkephalin, b-endorphin, dynorphin).
Structural levels:
I Primary (genetic sequences conditionality)
II Secondary
1. repetitive: a-heliks, b-pleated structure;
2. non-repetitive: spiral, omega-loop, random coil structures;
Supersecondary-most common patterns: bab, b-pin, aa-structure, b-barrel, a/b-barrel.
III Tertiary- non-covalent interactions responsible for stabilizing of 3D structure: electrostatic forces (dipole-dipole interaction, salt bridge), hydrogen bond, hydrophobic bond. A disulfide bond in stabilization of 3D protein structure;
IV Quaternary - thermodynamic stability of quaternary structure, topology of protein complexes (number and types of subunits, organization).
Domains-structural and functional specificity.
Stability of proteins in physiological conditions. Flexibility of protein structure.
Conformational changes of proteins in vitro (denaturation, renaturation). In vivo protein folding. Inadequately folded proteins (protein misfolding) as proteopathy (prion diseases);
Function as a consequence of structure of some fibrillar and globular proteins. Structure and function of myoglobin, keratin, collagen.
Lab
Proteins
Buffering effect of proteins; Reversible precipitation by salting out. Irreversible denaturation of proteins (thermal, by heavy metals, by pH change, with sulfosalicylic acid);
Reactions for qualitatitive determination of proteins (biuret, xanthoproteic, cysteine); determination of protein concentration (biuretic, Lowry's method, Bradford's method);
Acid hydrolysis of nucleoproteins and identification of components of nucleoproteins in hydrolysate
Bioinformatics of proteins
Way of using protein databases and available tools in finding basic information on the protein (PubMed and Expasy); Information on proteins in UniProtKB, especially on proteins involved in various diseases.
In silico prediction of basic properties of proteins; In silico hydrolysis/digestion of proteins; In silico prediction of protein secondary structure;
3D structure of proteins in Protein Data Bank (PDB); protein-ligand interactions, in particular, protein-drug interactions;
In silico prediction of post-translational modification (PTM).
Week VIII
Lecture and Seminar
Protein-ligand interactions; Proteins as biocatalysts; Basics of proteomics in medicine; Bioinformatics of protein; Carbohydrates
Protein-ligand interactions
Molecular bases of specific recognition and binding of ligand to protein-template hypothesis (key-lock model), model of induced adjustment;
Complementarity and stability of protein-ligand complex. Binding protein and ligand as an equilibrium process. Affinity constant and binding energy of protein and ligand.
Protein-ligand interactions and regulation of biological activity. Protein complexes-biological nanomachines.
Cooperative effect in hemoglobin. Hemoglobin-structure of protein subunits, the structure of heme. Oxygen binding-cooperative effect.
Proteins as biocatalysts. Specificity of enzymatic biocatalysis compared to non-biological catalysts. Specificity of the enzyme-substrate interaction in the light of key-lock and induced adjustment.
Basics of proteomics in medicine. Bioinformatics of protein
The principles of „large scale" protein analysis in the study of biological processes (considering disease at the level of proteins, proteins as drugs targets);
Comparative proteomics (comparison of normal and pathological proteome, disease monitoring, tracking the impact of drugs); Methods of structural and functional proteomics.
Bioinformatics of important medical proteins-databases and tools.
Carbohydrates
Structure of biologically important monosaccharides. Structural and stereoisomerism (D- and L-configuration); epimeric sugars; cyclization of monosaccharides and anomers.
Reactivity of monosaccharides as polyfunctional compounds:
1. Oxidation and formation of biologically important uronic acids and their lactone derivatives (gluconolactone, glucuronolactone);
2. Reduction and formation of biologically important polyhydroxy alcohols (sorbitol, mannitol);
3. Esterification of monosaccharides: phosphate esters of glucose (glucose-6-phosphate); phosphate esters of fructose (fructose-6-phosphate and fructose-1,6-diphosphate);
4. Formation of glycosides (a- and b-glycosidic bond)
Biologically important deoxy- (2-deoxy-D-ribose) and amino- derivatives of monosaccharides (glucosamine, galactosamine and their acylated molecules; N-acetylneuraminic acid);
Biologically important disaccharides (lactose, maltose, sucrose);
Polysaccharides:
1. Homopolysaccharides: glycogen-structure, characteristics and role; starch;
2. Heteropolysaccharides: glycosaminoglycans-structure, characteristics and roles, hyaluronic acid, chondroitin sulfate, heparin;
Glycoproteins (carbohohydrate residue bond to protein through formation of glycosidic bond: N-glycosylation of Asn and Gln, O-glycosylation of OH group from amino acids Ser, Thr); structure of proteoglycans.
Lab
Carbohydrates
Reduction properties of monosaccharides: Fehling's reaction with glucose and fructose.
Dehydration reaction of monosaccharides and formation of colored complexes with phenols: Molisch's and Seliwanoff's reaction with glucose, fructose (difference between pentoses and hexoses, aldoses and ketoses, respectively).
Disaccharides reaction (reducing and nonreducing disaccharides): Fehling's reaction with lactose; inversion of sucrose and Fehling's reaction with invert sugar.
Reactions of polysaccharides: gradual hydrolysis of starch, formation of dextrin and determination of hydrolysis products.
Week IX
Lecture and Seminar
Lipids, Nucleic acids
Lipids
Structures and properties of saturated fatty acids as constituents of lipids.
Structures and properties of the cis-unsaturated fatty acids; W-3 and W-6 fatty acids.
Structure of triacylglycerols and their function as energy reserves; hydrolysis of triacyglycerols in the presence of a lipase;
Structural features of aminoalcohols (colamine, choline, sphingosine), as constituents of phospholipids; Reactivity of the aminoalcohols in physiological conditions: oxidation of choline to betaine; acylation of choline and acetylcholine formation; hydrolysis of acetylcholine in the presence of choline esterase;
Structure of glycerophospholipids (phosphatidic acid, lecithin, cephalin) and their role in formation of biological membrane;
Structure of sphingolipids (ceramide, sphingomyelin, cerebroside, ganglioside) and their role in formation of biological membrane.
Aggregation of lipids and formation of micelles and bilayers; liposomes; structure and fluidity of plasma membrane.
Nucleic acids
Nomenclature of purine and pyrimidine bases, nucleosides and nucleotides. N-glycosidic bond in nucleosides and phosphoester bond in nucleotides. Importance of anhydride bond in di- and triphosphonucleotides (ADP, ATP). Cyclic nucleotides (cAMP), dinucleotides (NAD+, NADP+). Covalent bond of nucleotides by phosphodiester bond in polynucleotide chain.
Structure of DNA (1°, 2°). Importance of hydrogen bonds between complementary bases as transverse interactions and Van der Waal's forces between adjacent base pairs as vertical interactions in stabilization of 2° structure. Various forms of DNA molecules (A, B, Z). DNA damage: formation of dimers of pyrimidine bases. Structure and properties of histones, formation of nucleoproteins. Covalent modifications of DNA and histones-importance in gene regulation.
RNA structure (1°, 2°). RNA as catalysts. Specificities of catalysis by ribozymes. Importance of ribozymes for medicine.
Lab
Lipids
Reactions of triglycerides-alkaline hydrolysis of triglycerides; acrolein reaction of glycerol.
Reactions of fatty acids.
Colorimetric determination of cholesterol.
Qualitative test for bile acids.
1. A PRACTICAL GUIDE TO CHEMISTRY EXERCISES WITH WORKBOOK AND COLLECTION OF NUMERICAL PROBLEMS.
Authors: dr Kristina Gopčević, dr Vesna Vujić, dr Ksenija Stojanović, dr Vesna Dragutinović, dr Danijela Krstić, dr Nataša Avramović, dr Branimir Radosavljević, dr Lidija Izrael-Živković, Rade Bašić, School of Medicine, University of Belgrade, 5th Edition, 2016.
2. Chapters from the book „Fundaments of General, Organic and Biological Chemistry", McMurry, Ballantine, Hoeger, Peterson, Publisher: Pearson;8th Edition, 2016.
3. Chemistry: Online Preparatory Course-2017.
Elective courses are mandatory teaching methods. The student chooses two elective courses, one in winter and another in the summer semester. Number of students per elective course is limited.
Two elective courses from Chemistry in Medicine are offered to students of the I year of integrated studies in the II semester. These elective courses are highly recommended as a significant help for understanding and accomplishing regular courses in Chemistry in Medicine.
Elective course: Medically important chemical reactions through experiments and examples
Responsible Teacher: Assoc. Prof. Nataša Avramović, PhD
Teacher participants: Assoc. Prof. Nataša Avramović, PhD; Prof. Danijela Krstić, PhD; Assoc. Prof. Lidija Izrael Živković, PhD
Number of classes: 30 (15 classes of lectures (L) and 15 classes of practicals (P))
Number of students: up to 20
2nd Semester
Aims: The course is based on performing chemical reactions that take place in biological systems as well as the application of simple methods for the determination of medical important ions and compounds. Experiments are outlined to demonstrate the basic properties of biologically important ions and compounds, enabling their qualitative and quantitative analysis.
Course evaluation: Test (test consists of 5 questions: 3 theoretical + 2 calculations)
Curriculum 2023/2024 academic year, (II semester)
Term I Basics of the work in chemical laboratory (L + P)
Term II Stoichiometry through examples and experiments, Acids and bases (examples and chemical problems) (L + P)
Term III Acid-base equilibrium (experiments, examples, and chemical problems) (L + P), Lab: Determination of concentration of phosphoric acid using sodium hydroxide standard solution in the presence of methyl orange and phenolphthalein as indicators
Term IV Salts. Types of salts. Hydrolysis of salts (experiments); dissolution of poorly soluble salts (experiments); medical importance of some salts. Lab: Synthesis of some complexes; Ion reactions: Ca2+, Mg2+, Ba2+, Zn2+, Fe3+, Cl-, CO32-, SO42- (L + P)
Term V Spectrophotometry: Basic principles of colorimetry. Lab: Preparation of standard curve and determination of unknown concentration of phosphate PO43- ions in solution. (L + P)
Elective course: Chemistry in virtual laboratory
Responsible Teacher: Assoc. Prof. Lidija Izrael Živković, PhD
Teacher participants: Assoc. Prof. Lidija Izrael Živković, PhD; Prof. Kristina Gopcevic, PhD; Prof. Danijela Krstic, PhD; Assoc. Prof. Nataša Avramović, PhD, Assist. Prof. Ana Medić, PhD.
Number of classes: 30 (8 lectures, 12 seminars and 10 workshops)
Number of students: up to 20
2nd Semester
Aims: The course is based on Oxford Virtual Chemistry and Flash Animations-Essential Chemistry (McGraw Hill animations) and computer programs such as ChemBuddy-BATE and ACD/ChemSketch. Virtual laboratory enables students to acquire specialized knowledge and understanding of selected topics in chemistry at different levels. Selected topics are useful and interesting for students of Medicine. Through this course, students will become familiar with basic principles in chemistry, which will be valuable help during the further study of chemistry, biochemistry, and physiology. Through Chemistry in a virtual laboratory students will experience and learn chemistry in a new way.
Structure of the course: 5 terms are planned: The first four start with 2 hours of introducing lectures and 4 hours of workshops and seminars. Within the final, fifth term, students will present their seminar papers.
Course evaluation: During the course, students will solve different tasks on their own using computer and web tools, and in the final term each student will present a seminar paper.
Curriculum, 2023/2024 academic year
(II semester)
Term I Student will review and refresh their basic knowledge in general chemistry through animation and interactive quizzes. Virtual experiments will be performed using Oxford Virtual Chemistry.
Term II Basic calculations in chemistry; Students will have a list of tasks and internet addresses and available computer programs to perform different calculations in chemistry.
Term III Carbon in action; Students will repeat some of important reactions of organic compounds. They will be able to follow the reaction through animation/simulation of its mechanism. Students will have interactive quizzes as well.
Term IV Possibilities of internet gold mine to someone interested in the biological importance of various chemical substances; Use of „online" available bioinfo systems, where after introduction, each student (or group of up to 3 students) will make a search on compound based on its name or structural formula. Search will be performed on PubChem as a part of Entry bioinformatic system, with focuses on biological/medical importance of the compound and its structural specificity.
Term V Student seminar presentation
Assessment and evaluation of students
Maximum number of points obtained for Chemistry in Medicine Course is 100. Points are obtained according to the following model:
1) Colloquia and evaluation at seminars/practicals:
The maximum number of points obtained at colloquia in the fifth and tenth week of the course covering topics from General Chemistry, Organic Chemistry, and Chemistry of Natural Products is 96 points. Remedial colloquia are organized in the sixth and eleventh week of the winter semester and can be taken only by students who did not pass a regular term colloquium, and those with justified absence (decision of absence justification brought by the Course Director). Attendance points for all instruction forms and active participation in seminars and practicals are also recorded and included in the total number of points. A student passes the Chemistry exam if he passes all three areas (minimum 17 points per area, i.e., a total of 51 points).
2) If a student does not pass content from 3 areas of Chemistry (General Chemistry, Organic Chemistry, and Chemistry of Natural Products) during the regular course, he further takes colloquia from particular areas in corresponding terms. Each colloquium area is taken in separate exam terms. A student passes the entire course content if he collects a minimum of 51 points in three areas with a minimum of 17 points. The content colloquium passed is valid for 2 academic years.
Continuing student assessment involves points obtained for active participation and colloquia (points are saved in student's records and electronic database).
Points for student's active participation are obtained at seminars and practicals (maximum 9 points during 9 weeks). Active participation includes discussion, and providing an excellent answer (half a point is given by a teacher/associate who performs a seminar/practical). Attendance at lectures is also recorded in the following way: 0.5 points for 6 lecture presence, 1 point for 7 lecture presence, 1.5 points for 8 lecture presence, and 2 points for 9 lecture presence. Points for active participation are added to the total sum of points after passing the final exam (they are not taken into account for reaching the minimum number of points for the exam).
Colloquium points
I Colloquium, taken in a written form as a test, is held after 4 weeks of instruction and includes covered content. The test consists of multiple-choice questions and questions requiring thorough analysis. Tests include General Chemistry which is graded with 17 points, and the maximum number of points that a student could obtain is 32.
II Colloquium, taken in a written form as a test, is held after 9 weeks of instruction and includes the Organic Chemistry and Chemistry of Natural Products. Tests consist of multiple-choice questions and questions requiring thorough analysis. The tests are graded with 17 points and the maximum number of points that a student could obtain is 32, each.
The results of colloquia are saved in the student's records, and when a student passes all three areas the total number of points is written down in the student's transcript and recorded in the electronic database.