Protein Chemistry

1. Protein Chemistry

2.

3. Essential amino acids

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

4. Amino acids classification

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

5.

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

6.

5. Positively charged

7. Acid-base properties of amino acids

8. The primary structure of protein

The primary structure
of protein
peptide bonds

9. The determination of the primary structure

Method
Reagent
N-terminal Sanger’ s
2,4method Dinitrofluorobenzene
Edman’s
Phenylisithiocianate
metod
C-terminal Acabory’s
Hydrasin
method
Enzymatic
Carboxypeptidase

10. The determination of the primary structure

Reagent
Cyanogen bromide (CNBr)
Hydroxylamine
N-bromosuccinimide
Pepsin
Trypsin
Chymotrypsin
Amino acid
residues
Met
Asp Gly
Trp
Phe, Tyr, Glu
Arg, Lys
Trp, Tyr, Phe

11. The secondary structure of protein

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

12. The tertiary structure of myoglobin

The tertiary structure
of myoglobin

13. Types of bonds between amino acid radicals

Types of bonds between amino acid radicals

14. Chaperone

15. Participation of chaperones in protein folding

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

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

18.

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

19. Classification of proteins Simple proteins

20. Albumins and globulins

Serum albumin
Cashew globulin a powerful allergen

21. Hystones and DNA

22. Prolamin

23. Conjugative proteins

24. Chromoproteins Hemoproteins

Hemoglobin
Myoglobin

25. Hemoglobine structure

26. Bindig of oxygen by hemoglobin

Bindig of oxygen by hemoglobin

27.

28. Hemoglobinopathies Sickle cell anemia

29.

30. Abnormal hemoglobins

Abnormal hemoglobins
Type
Composition
Norm
HbС
HbD
2 2
2 2
Gly 6 in
Ley 28 in
HbН
4
Replacement
Lis
Gly

31. Flavoproteins

FAD
FMN

32. Lipoprotein structure

Lipoprotein structure

33. Covalent bond formation in phosphoprotein

Covalent bond formation
in phosphoprotein

34. Ionic bond formation in phosphoprotein

Ionic bond formation
in phosphoprotein

35. Glycoproteins Terminal carbohydrate

Glycoproteins
Terminal carbohydrate
N-acetylgalactosamine
fucose
sialic acid

36. Bond formation in glycoproteins

Bond formation
in glycoproteins
Serine
residue

37. The structure of  immunoglobulin

The structure of
immunoglobulin

38. Metalloproteins

Apoferritin
Ferritin

39. Metalloproteins

Transferrin
Linking center in
transferrin

40. Nucleoproteins Nucleic Acids

DNA
RNA
Nuclear
Messenger
Cytoplasmic
Transport
Ribosomal
Catalitic

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

Complementary
chains of DNA

44. Stacking interaction

Stacking interaction

45. The intensity of stacking

Purine – Purine >
> Pyrimidine – Purine >
> Pyrimidine – Pyrimidine

46. Cloverleaf model

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

47. t-RNA: L-shaped

48. Вiochemistry of enzymes

49. Enzymes are biological catalysts

50. Enzyme active site

51. Enzyme active site

52.

coenzyme binding domain
inactive enzyme
coenzyme
active enzyme

53.

The overall
Coenzyme
role
Coenzyme A Activation and
transfer of
acyl groups
Pyridoxal
transfer
of amino
phosphate
groups
Transfer of
FAD
hydrogen
(electrons)
Vitamin
precursor
Pantothenic
acid
Pyridoxine Vitamin B6
Riboflavin Vitamin B2

54. Allosteric enzyme

Allosteric enzyme
Active site
Allosteric
site

55. Bifunctional enzyme

Bifunctional enzyme
Kinase domain
Phosphatase domain

56. Isozymes of lactate dehydrogenase

57. Multimolecular enzyme systems

Multimolecular enzyme systems
NADPH oxidase

58.

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

59. Hermann Emil Fischer (1852 - 1919)

Hermann Emil Fischer (1852 - 1919)

60. Lock-and-key model by Fisher

E + S E-S E + P

61. Daniel Koshland (1920 - 2007)

Daniel Koshland (1920 - 2007)

62. Induced-fit theory by Koshlend

63. Substrate strain theory

64.

65. Leonor Michaelis

Enzyme kinetics
Leonor Michaelis
Maud Leonora Menten

66.

Michaelis – Menten
equation
Briggs – Haldane
equation:
max [ S ]
K m [S ]
Vmax [ S ]
KS [ S ]

67.

68. Lineweaver – Burk plot

69.

Enzymes are sensitive to temperature

70.

Enzymes are sensitive to pH

71.

72.

Enzymes are very specific and
only work with certain substrates

73. Urease 

Enzymes with absolute specificity
Urease
CO(NH2)2 + 2H2O = H2O + CO2 + 2NH3

74. Arginase

75. Pancreatic lipase

Enzymes with relative (group)
specificity
Pancreatic lipase

76. Fumarase

Stereo specificity
Fumarase
fumaric acid
maleic acid

77. Enzyme Classifcation

Group
Reaction catalyzed
Example(s)
Oxidation/reduction
EC 1
Dehydroreactions; transfer of H and O
Oxidogenase,
atoms or electrons from one
reductases
oxidase
substance to another
Transfer of a functional
EC 2
Transaminase
group from one substance to
Transferases
, kinase
another.
Formation of two products
EC 3
Lipase,
from a substrate
Hydrolases
peptidase
by hydrolysis

78. Enzyme Classifcation

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

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
cleave off the N-terminal
end from a tripeptide
Hydrolase
act on peptide bonds
cleave off the Nterminal amino acid from
a polypeptide

80. Metabolism regulation

Enzyme activity
Enzyme amount
Rate of chemical processes
Metabolites concentrations
Homeostasis and body functioning

81. Regulation of enzyme synthesis

82. Regulation of enzyme activity

Regulation of
enzyme activity

83. Enzymatic activity

IU = 1mcmole/min
1 kat = 1 mole/sec
1 IU = 16.67 nkat

84. Enzymes activators

Enzymes activators
Enzyme
Cytochromes
Amylase
Cholinesterase
Pancreatic lipase
Activator
Fe2+
2+
Ca , Cl
2+
Mn
Bile salts

85.

86. Competitive inhibition

Competitive inhibition

87.

malonate
succinate
fumarate

88.

p-aminobenzoic acid
sulfonamide

89.

Atorvastatin

90. Non-competitive inhibition

91.

92. Un-competitive inhibition

Un-competitive inhibition

93. Irreversible competitive inhibition

94. Irreversible competitive inhibition

95.

96. Feedback inhibition