Protein Chemistry презентация

Содержание

Слайд 2

Слайд 3

Essential amino acids valine, leucine, isoleucine, lysine, methionine, threonine, tryptophan,

Essential amino acids

valine, leucine, isoleucine, lysine, methionine, threonine, tryptophan,

phenylalanine

Semi-essential amino acids

arginine and histidine

Слайд 4

Amino acids classification Non-polar (hydrophobic) 2. Polar (hydrophilic)

Amino acids classification

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

Слайд 5

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

3. Aromatic (mainly non-polar)

4. Negatively charged

Слайд 6

5. Positively charged

5. Positively charged

Слайд 7

Acid-base properties of amino acids

Acid-base properties of amino acids

Слайд 8

The primary structure of protein peptide bonds

The primary structure of protein

peptide bonds

Слайд 9

The determination of the primary structure


The determination of the primary structure

Слайд 10

The determination of the primary structure


The determination of the primary structure

Слайд 11

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

The secondary structure of protein

α-helix

β-pleated sheet

hydrogen bonds

Слайд 12

The tertiary structure of myoglobin

The tertiary structure of myoglobin

Слайд 13

Types of bonds between amino acid radicals

Types of bonds between amino acid radicals

Слайд 14

Chaperone

Chaperone

Слайд 15

Participation of chaperones in protein folding

Participation of chaperones in protein folding

Слайд 16

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

The globular domains in the g-crystallin
(protein of human’s eye lens)

a random coil

Слайд 17

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

The quaternary structure of hemoglobin

α-chain

β-chain

heme

Слайд 18

I, II, III and IV – mitochondrial respiratory chain complexes

I, II, III and IV – mitochondrial respiratory chain complexes
(the electron transport

chain)

Fumarate

Succinate

inner mitochondrial membrane

intermembrane space

matrix

Слайд 19

Classification of proteins Simple proteins

Classification of proteins Simple proteins

Слайд 20

Albumins and globulins Serum albumin Cashew globulin - a powerful allergen

Albumins and globulins

Serum albumin

Cashew globulin - a powerful allergen

Слайд 21

Hystones and DNA

Hystones and DNA

Слайд 22

Prolamin

Prolamin

Слайд 23

Conjugative proteins

Conjugative proteins

Слайд 24

Chromoproteins Hemoproteins Hemoglobin Myoglobin

Chromoproteins Hemoproteins

Hemoglobin

Myoglobin

Слайд 25

Hemoglobine structure

Hemoglobine structure

Слайд 26

Bindig of oxygen by hemoglobin

Bindig of oxygen by hemoglobin

Слайд 27

Слайд 28

Hemoglobinopathies Sickle cell anemia

Hemoglobinopathies Sickle cell anemia

Слайд 29

Слайд 30

Abnormal hemoglobins

Abnormal hemoglobins

Слайд 31

Flavoproteins FMN FAD

Flavoproteins

FMN

FAD

Слайд 32

Lipoprotein structure

Lipoprotein structure

Слайд 33

Covalent bond formation in phosphoprotein

Covalent bond formation in phosphoprotein

Слайд 34

Ionic bond formation in phosphoprotein

Ionic bond formation in phosphoprotein

Слайд 35

Glycoproteins Terminal carbohydrate N-acetylgalactosamine fucose sialic acid

Glycoproteins Terminal carbohydrate

N-acetylgalactosamine

fucose

sialic acid

Слайд 36

Bond formation in glycoproteins Serine residue

Bond formation in glycoproteins

Serine
residue

Слайд 37

The structure of immunoglobulin

The structure of  immunoglobulin

Слайд 38

Metalloproteins Ferritin Apoferritin

Metalloproteins

Ferritin

Apoferritin

Слайд 39

Metalloproteins Transferrin Linking center in transferrin

Metalloproteins

Transferrin

Linking center in transferrin 

Слайд 40

Nucleoproteins Nucleic Acids

Nucleoproteins Nucleic Acids

Слайд 41

DNA polynucleotide chain structure B B B │ │ │

DNA polynucleotide chain structure

B B B
│ │ │
− S

− P − S − P − S −
Слайд 42

Chargaff’s rules A = T, G = C A +

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)
Слайд 43

Complementary chains of DNA

Complementary chains of DNA

Слайд 44

Stacking interaction

Stacking interaction

Слайд 45

The intensity of stacking Purine – Purine > > Pyrimidine

The intensity of stacking

Purine – Purine >
> Pyrimidine – Purine

>
> Pyrimidine – Pyrimidine
Слайд 46

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

Cloverleaf model

acceptor stem

D-loop

anticodon loop

variable loop

TPsiC-loop

CCA-3' of the
acceptor stem

anticodon

Слайд 47

t-RNA: L-shaped

t-RNA: L-shaped

Слайд 48

Вiochemistry of enzymes

Вiochemistry of enzymes

Слайд 49

Enzymes are biological catalysts

Enzymes are biological catalysts

Слайд 50

Enzyme active site

Enzyme active site

Слайд 51

Enzyme active site

Enzyme active site

Слайд 52

coenzyme binding domain inactive enzyme active enzyme coenzyme

coenzyme binding domain

inactive enzyme

active enzyme

coenzyme

Слайд 53

Слайд 54

Allosteric enzyme Active site Allosteric site

Allosteric enzyme

Active site

Allosteric site

Слайд 55

Bifunctional enzyme Kinase domain Phosphatase domain

Bifunctional enzyme

Kinase domain Phosphatase domain

Слайд 56

Isozymes of lactate dehydrogenase

Isozymes of lactate dehydrogenase

Слайд 57

Multimolecular enzyme systems NADPH oxidase

Multimolecular enzyme systems

NADPH oxidase

Слайд 58

I, II, III and IV – mitochondrial respiratory chain complexes

I, II, III and IV – mitochondrial respiratory chain complexes
(the electron transport

chain)

Fumarate

Succinate

inner mitochondrial membrane

intermembrane space

matrix

Слайд 59

Hermann Emil Fischer (1852 - 1919)

Hermann Emil Fischer (1852 - 1919)

Слайд 60

Lock-and-key model by Fisher E + S → E-S → E + P

Lock-and-key model by Fisher

E + S → E-S → E + P

Слайд 61

Daniel Koshland (1920 - 2007)

Daniel Koshland (1920 - 2007)

Слайд 62

Induced-fit theory by Koshlend

Induced-fit theory by Koshlend

Слайд 63

Substrate strain theory

Substrate strain theory

Слайд 64

Слайд 65

Leonor Michaelis Maud Leonora Menten Enzyme kinetics

Leonor Michaelis

Maud Leonora Menten

Enzyme kinetics

Слайд 66

Michaelis – Menten equation Briggs – Haldane equation:

Michaelis – Menten
equation

Briggs – Haldane
equation:

Слайд 67

Слайд 68

Lineweaver – Burk plot

Lineweaver – Burk plot

Слайд 69

Enzymes are sensitive to temperature

Enzymes are sensitive to temperature

Слайд 70

Enzymes are sensitive to pH

Enzymes are sensitive to pH

Слайд 71

Слайд 72

Enzymes are very specific and only work with certain substrates

Enzymes are very specific and only work with certain substrates

Слайд 73

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

CO(NH2)2 + 2H2O = H2O + CO2 + 2NH3

Urease 

Enzymes with absolute specificity

Слайд 74

Arginase

Arginase

Слайд 75

Pancreatic lipase Enzymes with relative (group) specificity

Pancreatic lipase

Enzymes with relative (group) specificity

Слайд 76

Fumarase fumaric acid maleic acid Stereo specificity

Fumarase

fumaric acid  maleic acid

Stereo specificity

Слайд 77

Enzyme Classifcation

Enzyme Classifcation

Слайд 78

Enzyme Classifcation

Enzyme Classifcation

Слайд 79

Enzyme Classifcation The Enzyme Commission number (EC number) is a

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

Слайд 80

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

Metabolism regulation

Rate of chemical processes

Metabolites concentrations

Enzyme activity

Enzyme amount

Homeostasis and body functioning

Слайд 81

Regulation of enzyme synthesis

Regulation of enzyme synthesis

Слайд 82

Regulation of enzyme activity

Regulation of enzyme activity

Слайд 83

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

Enzymatic activity

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

nkat
Слайд 84

Enzymes activators

Enzymes activators

Слайд 85

Слайд 86

Competitive inhibition

Competitive inhibition

Слайд 87

succinate fumarate malonate


succinate

fumarate

malonate

Слайд 88

p-aminobenzoic acid sulfonamide


p-aminobenzoic acid

sulfonamide

Слайд 89

Atorvastatin

Atorvastatin

Слайд 90

Non-competitive inhibition

Non-competitive inhibition

Слайд 91

Слайд 92

Un-competitive inhibition

Un-competitive inhibition

Слайд 93

Irreversible competitive inhibition

Irreversible competitive inhibition

Слайд 94

Irreversible competitive inhibition

Irreversible competitive inhibition

Слайд 95

Имя файла: Protein-Chemistry.pptx
Количество просмотров: 40
Количество скачиваний: 0