3. Essential amino acids valine, leucine, isoleucine, lysine, methionine, threonine, tryptophan, phenylalanine Semi-essential amino acids arginine and histidine

4. 1.Non-polar (hydrophobic) 2. Polar (hydrophilic)

5. 3. Aromatic (mainly non-polar) 4. Negatively charged

6. 5. Positively charged

8. The primary structure of protein peptide bonds

9. MethodReagent N-terminalSanger’ s method 2,4- Dinitrofluorobenzene Edman’s metod Phenylisithiocianate C-terminalAcabory’s method Hydrasin EnzymaticCarboxypeptidase The determination of the primary structure

10. ReagentAmino acid residues Cyanogen bromide (CNBr) Met Hydroxylamine Asp  Gly N- bromosuccinimideTrp PepsinPhe, Tyr, Glu TrypsinArg, Lys ChymotrypsinTrp, Tyr, Phe The determination of the primary structure

11. The secondary structure of protein  -helix β-pleated sheet hydrogen bonds

12. The tertiary structure of myoglobin

13. Types of bonds between amino acid radicals

14. Chaperone

15. Participation of chaperones in protein folding

16. The globular domains in the g-crystallin (protein of human’s eye lens) a random coil

17. The quaternary structure of hemoglobin α-chain β-chain heme

18. I, II, III and IV – mitochondrial respiratory chain complexes (the electron transport chain) FumarateSuccinate inner mitochondrial membrane intermembrane space matrix

20. Albumins and globulins Serum albumin Cashew globulin - a powerful allergen

21. Hystones and DNA

22. Prolamin

24. Chromoproteins Hemoproteins HemoglobinMyoglobin

25. Hemoglobine structure

26. Bindig of oxygen by hemoglobin

28. Hemoglobinopathies Sickle cell anemia

30. Abnormal hemoglobins TypeCompo- sition NormReplace- ment HbС 2222 Gly 6 in  Lis HbD 2222 Ley 28 in  Gly HbН 44

31. Flavoproteins FMN FAD

32. Lipoprotein structure

33. Covalent bond formation in phosphoprotein

34. Ionic bond formation in phosphoprotein

35. Glycoproteins Terminal carbohydrate N-acetylgalactosaminefucosesialic acid

36. Bond formation in glycoproteins Serine residue

37. The structure of immunoglobulin

38. Metalloproteins FerritinApoferritin

39. Metalloproteins Transferrin Linking center in transferrin

40. Nucleoproteins Nucleic Acids DNA NuclearCytoplasmic RNA MessengerTransportRibosomalCatalitic

41. DNA polynucleotide chain structure B B B │ │ │ − S − P − S − P − S −

42. Chargaff’s rules A = T, G = C A + G = C + T A + C = G + T (G + C) / (A + T) = 0,54 - 0,94 (in animals) = 0,45-2,57 (in microorganisms)

43. Complementary chains of DNA

44. Stacking interaction

45. The intensity of stacking Purine – Purine > > Pyrimidine – Purine > > Pyrimidine – Pyrimidine

46. Cloverleaf model acceptor stem D-loop anticodon loop variable loop TPsiC-loop CCA-3' of the acceptor stem anticodon

47. t-RNA: L-shaped

48. Вiochemistry of enzymes

49. Enzymes are biological catalysts

50. Enzyme active site

52. coenzyme binding domain inactive enzymeactive enzymecoenzyme

53. Coenzyme The overall role Vitamin precursor Coenzyme AActivation and transfer of acyl groups Pantothenic acid Pyridoxal phosphate transfer of amino groups Pyridoxine - Vitamin B 6 FADTransfer of hydrogen (electrons) Riboflavin - Vitamin B 2

54. Allosteric enzyme Active site Allosteric site

55. Bifunctional enzyme Kinase domain Phosphatase domain

56. Isozymes of lactate dehydrogenase

57. Multimolecular enzyme systems NADPH oxidase

58. I, II, III and IV – mitochondrial respiratory chain complexes (the electron transport chain) FumarateSuccinate inner mitochondrial membrane intermembrane space matrix

59. Hermann Emil Fischer (1852 - 1919)

60. Lock-and-key model by Fisher E + S  E-S  E + P

61. Daniel Koshland (1920 - 2007)

62. Induced-fit theory by Koshlend

63. Substrate strain theory

65. Leonor MichaelisMaud Leonora Menten Enzyme kinetics

66. Michaelis – Menten equation Briggs – Haldane equation:

68. Lineweaver – Burk plot

69. Enzymes are sensitive to temperature

70. Enzymes are sensitive to pH

72. Enzymes are very specific and only work with certain substrates

73. CO(NH 2 ) 2 + 2H 2 O = H 2 O + CO 2 + 2NH 3 Urease Enzymes with absolute specificity

74. Arginase

75. Pancreatic lipase Enzymes with relative (group) specificity

76. Fumarase fumaric acid maleic acid Stereo specificity

77. Enzyme Classifcation GroupReaction catalyzedExample(s) EC 1 Oxido- reductases Oxidation/reduction reactions; transfer of H and O atoms or electrons from one substance to another Dehydro- genase, oxidase EC 2 Transferases Transfer of a functional group from one substance to another. Transaminase, kinase EC 3 Hydrolases Formation of two products from a substrate by hydrolysis Lipase, peptidase

78. Enzyme Classifcation GroupReaction catalyzedExample(s) EC 4 Lyases Non-hydrolytic addition or removal of groups from substrates. C-C, C-N, C-O or C- S bonds may be cleaved Decarboxylase EC 5 Isomerases Intramolecule rearrangement, i.e. isomerization within a single molecule Glucose-6- phosphate isomerase EC 6 Ligases Join together two molecules by synthesis of new C-O, C-S, C-N or C-C bonds with breakdown of ATP Carboxylase

79. Enzyme Classifcation The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. Tripeptide aminopeptidase EC 3.4.11.4 Hydrolase act on peptide bonds cleave off the N- terminal amino acid from a polypeptide cleave off the N-terminal end from a tripeptide

80. Metabolism regulation Rate of chemical processes Metabolites concentrations Enzyme activityEnzyme amount Homeostasis and body functioning

81. Regulation of enzyme synthesis

82. Regulation of enzyme activity

83. Enzymatic activity IU = 1mcmole/min 1 kat = 1 mole/sec 1 IU = 16.67 nkat

84. Enzymes activators EnzymeActivator CytochromesFe 2+ AmylaseCa 2+, Cl  CholinesteraseMn 2+ Pancreatic lipaseBile salts

86. Competitive inhibition

87. succinate fumarate malonate

88. p-aminobenzoic acid sulfonamide

89. Atorvastatin

90. Non-competitive inhibition

92. Un-competitive inhibition

93. Irreversible competitive inhibition

96. Feedback inhibition