Semmelweis University

Department of Medical Chemistry Molecular Biology and Pathobiochemistry and Department of Medical Biochemistry

MEDICAL CHEMISTRY INFORMATION BULLETIN

2009-2010 Spring Semester

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Semmelweis University Department of Medical Chemistry, Molecular Biology and Pathobiochemistry and Department of Medical Biochemistry Course: Type:

Medical Chemistry Compulsory

Course director: Prof. Veronika Adam Teaching staff: Dr. László Szilák Prof. József Mandl Prof. Mária Sasvári Dr. Gergely Keszler Dr. László Csanády Dr. Nándor Müllner Dr. Pál Bauer Dr. Judit Bak Dr. Éva Keresztúri Dr. András Hrabák Dr. Tatjana Marta Stroe Dr. Tamás Mészáros Szpaszokukockaja Dr. Csaba Barta Dr. Miklós Csala Dr. Zsuzsanna Breuer Dr. Szabolcs Sipeki Dr. Attila Ambrus Dr. Zsolt Rónai

Teaching Secretary Student Affairs Secretary Lab coordinator Lab Staff

Dr. András Hrabák Tel.: (+36-1) 459-1500/ext. 60181 Email: [email protected] Mrs Katalin Nemes Tel: 459-1500/ext. 60061 Dr. Gergely Keszler

Mrs Mária Kövecses Mrs Márta Stroe Mrs Kinga Pelczer

Course timing Year: Period: Total weeks: Hours per week:

1st 2nd semester lecture 14 , seminar lecture 4 , seminar -

, practical 14 , practical 4

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The aim of the course: Medical Chemistry gives a comprehensive description and understanding of chemical structures and processes important in human body. These principles are necessary for the medical practice and for the learning of biochemistry. The informations also contribute to the learning of physiology, pathophysiology, pathology, pharmacology, numerous clinical topics and laboratory diagnostics. The main topics of this semester's course are the general, inorganic and organic chemistry. The pH and buffers, oxidation-reduction processes and the structures of biologically important organic molecules are particularly discussed. Special emphasis is put on medical aspects. Skills in experimental work are also developed during laboratory programs. Content:

Bioorganic chemistry I.

Amino acids, proteins and enzymes

II.

Carbohydrates

III.

Lipids

IV.

Nucleotides, nucleic acids

V.

Coenzymes, vitamins

VI.

Bioenergetics

Recommended books and handouts Lehninger-Nelson-Cox: Principles in Biochemistry Sasvári-Müllner: Bioorganic compounds II. (manuscript) Practical: Hrabák: Selected Collection of Chemical Calculations (manuscript) Medical Chemistry and Biochemistry Laboratory Manual (manuscript) Manuscripts can be bought in the shop of the Semmelweis Publisher (Nagyvárad tér) Students' own lecture notes See also the recommended books and handouts of the fall semester.

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Medical Chemistry I. for first year students. Schedule of Medical Chemistry Lectures. 2009-2010., Spring Semester Lectures

Monday Friday

13.00-14.40 12.10-13.50

Szent-Györgyi Lecture Hall Szent-Györgyi Lecture Hall

DD:MM

Topic(s)

Lecturer

1-5 February

Amino acids. Amino acids as electrolytes. Structure and chirality of amino acids. Reactions of amino acids. Proteins. The peptide bond. Structure levels in proteins. Conformation of proteins. Purification of proteins. Myoglobin and hemoglobin. Structural characteristics of fibrous proteins. Collagen. Enzymes. Enzymes as proteins, enzyme activity. Enzyme kinetics. Mechanism of action of some important enzymes (serine proteases). Reversible and irreversible inhibitions of enzymes. Regulation of enzyme activity. Carbohydrates. Monosaccharides. Classification, chirality, reactions. Disaccharides. Homo- and heteropolysaccharides. Biological roles of carbohydrates. Glycoproteins, glycolipids. Lipids. Classification, neutral lipids, fatty acids. Glycerophospholipids. Sphingolipids, blood group antigens, cerebrosides, gangliosides.

Mária Sasvári

Steroids. Cholesterol, structure, functions. Isoprene and isoprenoids.Bile acids. Calcitriol. Steroid hormones and their biological functions. Eicosanoids and their biological functions. Lipid-soluble vitamins. SPRING HOLIDAY Structure and nomenclature of ribo- and deoxyribonucleosides and -nucleotides. Base, nucleoside and nucleotide analogues, minor and rare bases and their importance. Nucleic acids, their biological roles, general structural features. Primary structure of nucleic acids. Three dimensional structure of DNA. Its role in the biological function. Analysis of DNA (electrophoresis, blotting, sequencing). Three dimensional structure of various RNAs. The genetic code, codons and anticodons. Exo- and endonucleases and their role in DNA and RNA metabolism. Compounds of B-vitamin complex, Vitamin C and their biological roles. Thiamine, riboflavine, pyridoxine, cobalamine and their coenzyme derivatives. Vitamins belonging to nucleotides (CoA, NAD(P), FAD). Their role as coenzymes in the hydrogen or acyl group transfer. Other water soluble vitamins (folic acid, biotin). Their structure and function as coenzymes. Group transfer potential. Coupled reactions in the metabolism. The phosphoryl transfer. Role of high energy phosphates in the intermediary metabolism. ATP. Formation of acetyl CoA from pyruvate. The pyruvate dehydrogenase complex. Regulation of the pyruvate dehydrogenase.

Csaba Barta

8-12 February 15-19 February 22-26 February

1 March 5-8 March

19 March

22-26 March

29 March -5 April 9 April

12-16 April

19 April

23-26 April

Mária Sasvári Mária Sasvári Mária Sasvári

Mária Sasvári András Hrabák

András Hrabák

Gergely Keszler

Gergely Keszler

Miklós Csala

Prof. József Mandl

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30 April- 3 May

Reactions of citric acid cycle. Enzymes and coenzymes. Prof. József Mandl Localization, regulation and significance of citric acid cycle. Glycolysis. Reactions, allosteric regulation, biological significance.

7 May

Mitochondrial membranes and their permeability. Miklós Csala Mitochondrial transporter systems. The respiratory chain: components, organization, function, inhibitors.Respiratory control, P/O ratio, uncoupling of oxidative phosphorylation. Mitochondrial ATPase. (FoF1-ATP-ase): structure, function, Miklós Csala inhibitors. Mechanism of oxidative phosphorylation. Chemiosmatic hypothesis. Mitochondrial transport of reducting equivalents. Energetics of the complete oxidation of glucose. Oxidoreductases - classification, general characteristics. Redox cycles of the coenzymes, NAD, NADP, FAD, glutathion.

10-14 May

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Program of laboratory practice in chemistry, Spring Semester, 2009-2010 Week

Period

1. 2. 3.

1-5 February 8-12 February 15-19 February

4.

22-26 February

5. 6. 7.

1-5 March 8-12 March 15-19 March

Experiment or program . Proteins I. Proteins II. Electrometric titration of amino acids* Thin layer chromatography* Consultation. Carbohydrates Consultation.

8.

22 -26 March

Midterm exam I.

SPRING HOLIDAY Gel chromatography* Gel electrophoresis, Western blot* 11. 19-23 April Studies on urease* 12. 26-30 April Consultation 13. 3-7 May Midterm exam II. 14. 10-14 May Lipids. Midterm III. (laboratory practice). * according to a schedule published elsewhere 9. 10.

•

29 March -5 April 6-9 April 12-16 April

homepage: www.biokemia.sote.hu

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Medical Chemistry I. for first year students. Laboratory teachers and dates. 2009-2010, Spring Semester (Family Names by Bold Characters) Group

Name of the teacher

Date of the lab program

EM/1 EM/2 EM/3 EM/4 EM/5 EM/6 EM/7 EM/8 EM/9 EM/10 EM/11 EM/12 EM/13 EM/14

Mészáros Tamás Csala Miklós Bak Judit Müllner Nándor Barta Csaba Szpaszokukockaja Tatjana Keszler Gergely Csanády László Stroe Márta Sasvári Mária Szilák László Szpaszokukockaja Tatjana Rónai Zsolt Sipeki Szabolcs

Wednesday 12.50-15.50 Thursday 8.00-11.00 Wednesday 9.40-12.40 Tuesday 8.00-11.00 Wednesday 9.40-12.40 Monday 8.00-11.00 Monday 8.00-11.00 Tuesday 14.30-17.30 Wednesday 9.40-12.40 Monday 8.00-11.00 Monday 15.00-18.00 Friday 14.50-17.50 Wednesday 9.40-12.40 Friday 14.10-17.10

ED/1 ED/2 ED/3 ED/4

Bauer Pál Ambrus Attila Breuer Zsuzsa Keresztúri Éva

Thursday 11.45-14.45 Thursday 11.45-14.45 Friday 14.50-17.50 Thursday 14.30-17.30

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Requirements of the department Practical lessons and seminars The practical classes and the seminars are an essential part of the medical course in biochemistry. Thus, the Department requires satisfactory attendance throughout the practical course as a condition of the examination. If anybody has four or more absences for whatever reason, we can not acknowledge their semester. Grading of the performance of laboratory work Lab work performance assessment is a part of the semifinal exam. The practical work and its documentation is assessed by the teachers at the end of each lesson. Laboratory exam is held on the last week of the semester. Students get one question from the List of Laboratory Questions and answer it in written form (in 30 min). The answers are assessed by the lab teachers and graded by 0 (failure) -3 scores. Midterm exams Students have to sit for midterm examinations before the examination period. Failed midterms can be retaken once, in a time scheduled by the laboratory teacher. The midterm questions should be answered in written form in 120 min according to the schedule of the practical lessons. The midterms are evaluated with grades from 0 up to 3 scores. The topics for the 1st midterm are those covered by the first 10 lectures (bioorganic chemistry topic list I. 1-18 questions) and the seminars of the first 5 weeks, whereas for the second one the questions II. 19-42. and III. 43-49. of the bioorganic chemistry topic list and seminars of weeks #7 through #12. Biochemical calculations will also be included in the first midterm. Both midterm exams can be retaken before the examination period. A recommended date is given on week 14. Third midterm exam is scheduled for the last (15th) week, including all the laboratory experiments of the second semester. This midterm exam cannot be retaken and its time is shorter (30 min). Final exam The grade of the semifinal exam is based on two elements: 1) theoretical written test (50 multiple choice questions and 10 structures); 2) bonus points collected in the course of the semester. The material of the final examination involves both the fall and the spring semesters’ topics. 20 multiple choice questions and 2 structures will be selected from the first semester in the written test !!! A topic list of the bioorganic chemistry is given at the end of this bulletin. These questions are used for the midterms and as an informative collection about the material of the spring semester. They are not final exam questions in this year. 1) The test consists of 60 questions (50 multiple choice and 10 structural formulae), which should be answered in 150 min. The topics covered by the test are enclosed (the topics of the first semester see in the previous bulletin). These are based on the recommended textbooks and the lectures. The exam can be passed only if the student collects at least 31 points from this part (each correctly answered question means 1 point for the score). 2) Bonus points (maximal number 9) can be collected in the course of the semester according to the following scheme: - from the midterm exams; 0-9 points, according to the sum of scores obtained; the third midterm is of the laboratory practice Grades of the semifinal exam Total score from the 3 elements of the semifinal 0-30 31-39 40-49 50-59 60-69

Grade 1 (not passed) 2 3 4 5 8

Competition Chemistry competition will be organized in the last period of the Semester (May). The best students (usually producing 70 % of the scores) will get exemption from the final written examination (with mark 5). This exemption is the authority of Prof. Adam and will be published in the last week. Dates for final exams. Exams are held on Wednesdays (and an additional day in the last week) with maximal number of 50 students (Medical + Dentist) per day. Applications should be submitted through the University administration system Neptun. Unsuccessful exams can be repeated after 5 days. Exemptions from final exams. Those students who would like to be being exempted from taking the biochemistry course on the basis of their previous studies are kindly asked to present their documents to the teaching secretary (or to dr. A. Hrabak) until 13 February. Students with the proper academic background are entitled to sit for a checking examination in written form (multiple choice test plus structures as in the semifinal exam). In case of successful examination the exemption will be granted by the department. The date of exam will be fixed later possibly at the end of February. For the material see the topic and structure lists.

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LIST OF TOPICS FOR THE MIDTERMS ALSO INDICATING THE MATERIAL OF THE BIOORGANIC PART OF THE FINAL EXAMINATION.

Groups of questions: Group I. Amino acids, Proteins, Enzymes Group II. Carbohydrates, lipids, nucleic acids,coenzymes Group III. Bioenergetics. Please find enclosed the list of obligatory structural formulas as well. These list serves as a help to prepare for the final exam and also as a source for the questions for midterm examinations. CHEMISTRY PRACTICAL QUESTIONS (for the laboratory midterm). 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14.

Reversible precipitation of proteins. Irreversible precipitation of proteins. Quantitative colorimetric determination of proteins (biuret, Ellmann). Gel filtration. Separation of proteins from potassium iodide. Paper and thin layer chromatography of amino acids. Principle of gel electrophoresis and western blotting. Electrometric titration of amino acids. Construction of the saturation curve of urease. Inhibition of urease activity. Reduction probes of carbohydrates. Carbohydrate reactions based on dehydration. Determination of glucose concentration by orto-toluidine. Determination of starch concentration by Lugol solution. Qualitative reactions of lipids

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Bioorganic chemistry Group I. Amino acids, proteins, enzymes (1-18.) 1. Neutral amino acids: Optical activity (enantiomers, diastereomers). Grouping principles (aliphatic and aromatic side chains, branched chain amino acids, sulfur containing amino acids). Hydropathy index. Acid-base character of neutral amino acids (protonic equilibria, isoelectric point, titration curve of alanine). 2. Neutral amino acids: polar side chains. Hydrogen bonds between side chains (examples!). Aromatic side chains in amino acids: their hydrophobic or hydrophilic character. Post-translational modification of amino acids (hydroxylation, phosphorylation). Biologically important derivatives of thyrosine (thyroxine, dopamine, noradrenaline, adrenaline). Biogen amines. 3. Acidic amino acids. Calculation of isoelectric point. Titration curve of aspartic acid. Comparison of acidity of different side chains and the -carboxyl group. Amides of aspartic and glutamic acid. 4. Basic amino acids. Calculation of isoeletric point.. Comparison of basicity of amine and imine groups in amino acids. Titration curve of arginine. Which of common amino acids has buffering capacity at neutral pH? 5. Peptides. Formation and properties of the peptide bond (cis and trans configuration of a peptide bond). Ionic side chains, possible charges on a peptide, dependence of the net charge on pH. Isoelectric point of peptides and proteins. The structure of glutathion. 6. Proteins: conformation. Definition of primary, secondary, tertiary and quaternary structure, types of bonds and interactions at each level. Ramanchandran plot. helix, parallel and antiparallel sheets. 7. Fibrous proteins. a-keratin, silk fibroin and collagen. The collagen helix. Post-translational modification (hydroxylation). Defective hydroxylation in scurvy. Procollagen, tropocollagen, collagen fiber (nature of Lys cross-links). 8. Myoglobin. Structural features of the globin chain. Formula of heme, oxidation state of iron. Function of proximal and distal histidine. 9. Hemoglobin as an allosteric protein. Oxygen saturation curves for myoglobin and hemoglobin: a comparison. Function of BPG. The Bohr-effect and its molecular mechanism. Conformational changes during oxygenation. 10. Effect of altered amino acid sequence on protein function. Normal human hemoglobin chains, comparison of fetal form to adult forms. Abnormal human hemoglobins: neutral and harmful mutation. HgM. HbS and the sickle cell anemia. 11. pH and temperature dependence of enzyme activity. Effect of charged groups in the active center on the pH profiles of enzymes. Definition of enzyme activity, specific enzyme activity and turnover number. Clinical importance of enzyme assays (nonfunctional plasma enzymes). 12. Effect of the enzyme on the equilibrium and on the activation energy. Transition states. The active center of the enzymes (lock and key model, induced fit model). Acid/base and covalent catalysis. 13. Serine proteases. Proteolytic activation of zymogens. Reaction mechanism: tetrahedral transition states. Specificity of proteases (chymotrypsin,trypsin, elastase). Specific inhibitor of Ser proteases (DIPF). 11

14. The Michaelis Menten model of enzyme kinetics. Initial rate. The Michaelis constant. Maximal velocity. Graphic evaluation of Vmax and KM. 15. Isoenzymes. Definition, examples (glucokinase-hexokinase, lactate dehydrogenases). 16. Reversible inhibition of enzymes. Competitive and non-competitive inhibition. 17. Control of enzyme activity by allosteric activation/inactivation. Kinetics of allosteric enzymes (K type and V type enzymes). Homotrope and heterotrop cooperativity (e.g. aspartate transcarbamoylase). 18. Control of enzyme activity by reversible covalent modification. Post-translational modification of proteins (phosophorylation). Protein kinases and protein phosphatases. Complex regulation (e.g. phosphorylase kinase).

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Group II. Carbohydrates, lipids, nucleic acids (19-46.) 19. Monosaccharides: functional groups, hemiacetal formation, conformation of pyranose and furanose rings. Structural formula of some important aldose: D-L glyceraldehyde, erythrose, ribose, deoxyribose, glucose, mannose, galactose. 20. Asymmetric carbon atoms in monosaccharides, mutarotation, anomeric sugars. The structure of alfa-D-glucopyranose and beta-D-fructofuranose. Structural formula of important ketoses (dihydroxyacetone, ribulose, xylulose, fructose) and other sugars (L 301-306, lecture). 21. Derivatives of sugars: deoxy sugars, amino sugars and their N-acetyl derivatives. O- and Nglycosides. Structural formula of deoxyribose, fucose, N-acetyl-glucosamine, N-acetyl-Dgalactosamine, sialic acid. Sugar phosphate esters . 22. Disaccharides: reducing and non-reducing disaccharides. Structure of sucrose, maltose, cellobiose and lactose. 23. Polysaccharides I. structure of important homopolysaccharides (glycogen, starch, dextran, cellulose). 24. Polysaccharides II. Structure of important heteropolysaccharides and their role in the living organism. 25. Fatty acids: nomenclature, function, classification. Saturated and unsaturated fatty acids. Essential fatty acids; function, physical properties Triacylglycerols, structure, function. Stereochemical numbering, prochirality. 26. Phosphoglycerolipids: structure, function. Selected representatives. Ether phospholipids. Plasmalogens. 27. Phosphosphingolipids: structure, function. Glycosphingolipids. Blood group antigens (ABO). 28. Cholesterol and its reduced derivatives, nomenclature, stereochemical structure. Bile acids (primary, secondary, conjugated bile acids): structure and function. Application of their detergent effect . 29. Steroid hormones. Structure, function. Vitamin D3 and its biologically active derivatives. 30. Isoprene and its biologically active derivatives. Lipid soluble vitamins. Vitamin K2, vitamin E. their functions. Vitamin A and its derivatives, function. Coenzyme Q: reduced and oxidized form. Dolichol phosphate, role in glycoprotein synthesis. 31. Arachidonic acid: structure. Eicosanoids: classification, functions(L. 258-259, lecture). 32. Membranes: fluidity, asymmetry, liposomes. Covalent lipid-protein conjugates: function, selected representatives. 33. Ribo- and deoxyribonucleosides and -nucleotides. Their structure and nomenclature. 34. Biological function of nucleotides (cyclic nucleotides, ATP, UDP-glucose cADP-ribose). 35. Base, nucleoside and nucleotide analogues, minor and rare bases and their importance. 13

36. Nucleic acids, their biological roles, general structural features. Primary structure of nucleic acids. 37. Three dimensional structure of DNA. Its role in the biological function. 38. Analysis of DNA(electrophoresis, blotting, sequencing). 39. Three dimensional structure of various RNAs. The genetic code, codons and anticodons. 40. Exo- and endonucleases and their role in DNA and RNA metabolism. 41. Compounds of B-vitamin complex, Vitamin C and their biological roles. Thiamine, riboflavine, pyridoxine, cobalamine and their coenzyme derivatives. 42. Vitamins belonging to nucleotides (CoA, NAD(P), FAD). Their role as coenzymes in the hydrogen or acyl group transfer. Other water soluble vitamins (folic acid, biotin). Their structure and function as coenzymes. Group III. Bioenergetics (43.-55.) 43. Group transfer potential. Coupled reactions in the metabolism. 44. The phosphoryl transfer. Role of high energy phosphates in the intermediary metabolism. ATP. 45. Formation of acetyl CoA from pyruvate. The pyruvate dehydrogenase complex. Regulation of the pyruvate dehydrogenase. 46. Reactions of citric acid cycle. Enzymes and coenzymes. 47.Localization, regulation and significance of citric acid cycle. 48. Glycolysis. 1st phase. 49. Glycolysis - 2nd phase. 50. Mitochondrial membranes and their permeability. Mitochondrial transporter systems. 51. The respiratory chain: components, organization, function, inhibitors. 52. Respiratory control, P/O ratio, uncoupling of oxidative phosphorylation. 53. Mitochondrial ATPase. (FoF1-ATP-ase): structure, function, inhibitors. Mechanism of oxidative phosphorylation. Chemiosmatic hypothesis. 54. Mitochondrial transport of reducting equivalents. Energetics of the complete oxidation of glucose. 55. Oxidoreductases - classification, general characteristics. Redox cycles of the coenzymes, NAD, NADP, FAD, glutathion.

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The structures of the following compounds are highly recommended to know at the final exam: Inorganic compounds:* Water, sodium chlorate, potassium permanganate, sodium thiosulfate, silver nitrate, silver chromate, sodium chloride, sulfuric acid, sodium nitrite, potassium nitrate, hydrochloric acid, sodium hydroxide, potassium sulfite, potassium hydroxide, potassium hydrogencarbonate, sodium carbonate, potassium biiodate, potassium iodide, bromous acid, sulfurous acid, hypochlorous acid, sodium hypochlorite, calcium chloride, magnesium sulfate, copper sulfate, zinc chloride, calcium sulfate, manganese chloride, mercury chloride, mercurous chloride (calomel), silver chloride, hydrogen cyanide, potassium ferricyanide, metaphosphoric acid, orthophosphoric acid, sodium dyhidrogen phosphate, dipotassium hydrogen phosphate, sodium pyrophosphate, hydrogen sulfide, ammonium sulfate, ferrous ammonium sulfate, hydrogen peroxide, nitrous acid, nitric acid, nitrous oxide, nitric oxide, carbon monoxide, carbon dioxide, sulfur dioxide, sulfur trioxide, perchloric acid, sodium chlorite, sodium periodate, aluminium chloride, potassium cyanide, hydroxylamine, ammonia, hydrazine, superoxide anion, boric acid, hydroxyapatite, fluoroapatite. Aromatic rings: benzene, naphtalene, phenantrene, pyrrole, thiophene, furane, thiazole, oxazole, imidazole, pyrazole, pyridine, pyrane, pyrazine, pyrimidine, purine, indole, pteridine, acridine. Basic organic compounds: methanol, ethanol, propanol, butanols, ethylene glycol, glycerol, inositol, phenol, diethylether, formaldehyde, acetaldehyde, acetone, mercaptoethanol, aniline, urea, guanidine. Organic acids: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, oxalic acid, malonic acid, succinic acid, glutaric acid, adipic acid, maleic acid, fumaric acid, lactic acid, βhydroxybutyric acid, pyruvic acid, acetoacetic acid, citric acid, cis-aconitic acid, isocitric acid, αketoglutaric acid, malic acid, oxaloacetic acid, tartaric acid. Types of bondings and derivatives: ether (phenolether), thioether, ester, lactone, thioester, anhydride (including mixed and phosphoric acid anhydrides), hemiacetale, hemiketale (cyclic forms included), Schiffbase, oxime, hydrazone, hydroxamic acid, amide, thiol, sulfonic acid. Amino acids and derivatives: glycine, alanine, valine, leucine, isoleucine, phenylalanine, tyrosine, tryptophane, cysteine, methionine, serine, threonine, lysine, arginine, histidine, aspartic acid, asparagine, glutamic acid, glutamine, proline, cystine, β-alanine, ornithine, citrulline, homocysteine, homoserine, ethanolamine, choline, histamine, epinephrine, serotonin, thyroxine. Lipids: palmitic acid, stearic acid, palmitoleic acid, oleic acid, linoleic acid, linolenic acid, arachidonic acid, diacyland triacylglycerols, phophatidic acid, phosphatidyl-ethanolamine, phosphatidyl-choline, phosphatidyl-serine, phosphatidyl-inositol, platelet activating factor, sphingosine, sphingomyelin, cholesterol, cortisol, aldosterone, estradiol, testosterone, progesterone, cholic acid, taurocholic acid, isoprene, β-carotene, prostaglandin E2. Carbohydrates: D- and L-glyceraldehyde, dihydroxyacetone, erythrose, treose, ribose, deoxyribose, glucose, mannose, galactose, fructose, ribulose, xylulose, maltose, cellobiose, lactose, sucrose, N-acetyl-glucosamine, Lfucose, sialic acid, aldonic and uronic acids, UDP-glucose, structural unit of starch and glycogen, structural unit of hyaluronic acid, chondroitin-sulfates and heparine. Nucleotides: adenine, guanine, cytosine, uracil, thymine, hypoxanthine, xanthine, uric acid, nucleosides and nucleotides formed of the bases mentioned previously, a structural unit of ribo- and deoxyribonucleic acid, pseudouridine, 5-fluorouracil, 5- bromouracil, 6-mercaptopurine. Vitamins and coenzymes: thiamine (and its pyrophosphate), riboflavine (FAD), nicotinamide (NAD, NADP and their reduced forms), pyridoxal phosphate, coenzyme A, coenzyme Q, vitamin A, vitamin D3, ascorbic acid, folic acid, tetrahydrofolic acid, biotin, porphyrine backbone.

* Inorganic structures will not be asked in the 10-structures sheet at the final exam. However, some of them may be involved in the 20 multiple choice questions of the first semester. 15