Protein Chemistry презентация

Содержание

Слайд 3

Essential amino acids

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

Semi-essential amino

acids

arginine and histidine

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Amino acids classification

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

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3. Aromatic (mainly non-polar)

4. Negatively charged

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5. Positively charged

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Acid-base properties of amino acids

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The primary structure of protein

peptide bonds

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The determination of the primary structure

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The determination of the primary structure

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The secondary structure of protein

α-helix

β-pleated sheet

hydrogen bonds

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The tertiary structure of myoglobin

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Types of bonds between amino acid radicals

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Chaperone

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Participation of chaperones in protein folding

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

a random coil

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The quaternary structure of hemoglobin

α-chain

β-chain

heme

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

Fumarate

Succinate

inner mitochondrial membrane

intermembrane

space

matrix

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Classification of proteins Simple proteins

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Albumins and globulins

Serum albumin

Cashew globulin - a powerful allergen

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Hystones and DNA

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Conjugative proteins

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Chromoproteins Hemoproteins

Hemoglobin

Myoglobin

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Hemoglobine structure

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Bindig of oxygen by hemoglobin

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Hemoglobinopathies Sickle cell anemia

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Abnormal hemoglobins

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Flavoproteins

FMN

FAD

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Lipoprotein structure

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Covalent bond formation in phosphoprotein

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Ionic bond formation in phosphoprotein

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Glycoproteins Terminal carbohydrate

N-acetylgalactosamine

fucose

sialic acid

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Bond formation in glycoproteins

Serine
residue

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The structure of  immunoglobulin

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Metalloproteins

Ferritin

Apoferritin

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Metalloproteins

Transferrin

Linking center in transferrin 

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Nucleoproteins Nucleic Acids

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DNA polynucleotide chain structure

B B B
│ │ │
− S − P

− S − P − S −

Слайд 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)

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Complementary chains of DNA

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Stacking interaction

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The intensity of stacking

Purine – Purine >
> Pyrimidine – Purine >
> Pyrimidine

– Pyrimidine

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Cloverleaf model

acceptor stem

D-loop

anticodon loop

variable loop

TPsiC-loop

CCA-3' of the
acceptor stem

anticodon

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t-RNA: L-shaped

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Вiochemistry of enzymes

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Enzymes are biological catalysts

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Enzyme active site

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Enzyme active site

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coenzyme binding domain

inactive enzyme

active enzyme

coenzyme

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Allosteric enzyme

Active site

Allosteric site

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Bifunctional enzyme

Kinase domain Phosphatase domain

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Isozymes of lactate dehydrogenase

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Multimolecular enzyme systems

NADPH oxidase

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

Fumarate

Succinate

inner mitochondrial membrane

intermembrane

space

matrix

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Hermann Emil Fischer (1852 - 1919)

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Lock-and-key model by Fisher

E + S → E-S → E + P

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Daniel Koshland (1920 - 2007)

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Induced-fit theory by Koshlend

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Substrate strain theory

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Leonor Michaelis

Maud Leonora Menten

Enzyme kinetics

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Michaelis – Menten
equation

Briggs – Haldane
equation:

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Lineweaver – Burk plot

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Enzymes are sensitive to temperature

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Enzymes are sensitive to pH

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Enzymes are very specific and only work with certain substrates

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CO(NH2)2 + 2H2O = H2O + CO2 + 2NH3

Urease 

Enzymes with absolute specificity

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Pancreatic lipase

Enzymes with relative (group) specificity

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Fumarase

fumaric acid  maleic acid

Stereo specificity

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Enzyme Classifcation

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Enzyme Classifcation

Слайд 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

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Metabolism regulation

Rate of chemical processes

Metabolites concentrations

Enzyme activity

Enzyme amount

Homeostasis and body functioning

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Regulation of enzyme synthesis

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Regulation of enzyme activity

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Enzymatic activity

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

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Enzymes activators

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Competitive inhibition

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succinate

fumarate

malonate

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p-aminobenzoic acid

sulfonamide

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Atorvastatin

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Non-competitive inhibition

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Un-competitive inhibition

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Irreversible competitive inhibition

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Irreversible competitive inhibition

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