Download a biology presentation on proteins. Protein molecule structure

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Simple proteins (proteins consisting only of amino acids)

ALBUMINS: are part of animal and plant tissues; found in egg whites, blood serum, milk, and plant seeds. GLOBULINS: are part of the cytoplasm, blood plasma and lymph (higher animals and humans), determining the immune properties of the body. HISTONES: Contained in the nuclei of most animal cells. GLUTELINS: found in cereal seeds and green parts of plants. PROLAMINS: simple storage proteins found only in cereal seeds. PROTAMINS: low molecular weight proteins contained in the nuclei of sperm in fish and birds. PROTENOIDS: proteins of animal origin, perform supporting functions in organisms.

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Complex proteins (contain amino acids and other compounds)

GLYCOPROTEIDS: contain carbohydrate LIPOPROTEIDS: contain complexes of proteins and lipids NUCLEOPROTEIDS: complexes of nucleic acids and proteins PHOSPHOPROTEIDS: contain complex proteins with a phosphoryl group –PO32- CHROMOPROTEIDS: contain colored non-protein groups

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Protein synthesis

In 1955, the structure of insulin was elucidated. Following this, the primary structure of ribonuclease, hemoglobin, trypsin and a number of other proteins was discovered. By chemical synthesis, complex peptides with the properties of hormones were first obtained, then it was possible to synthesize the hormone insulin, and finally the enzyme ribonuclease. Right chemical formula insulin and ribonuclease was confirmed by the fact that the synthetic proteins did not differ from the proteins produced by the body. The structure of over 200 proteins has now been fully or partially established.

Protein structure

Biology. Proteins are the most important components of cells. Plan. Determination of protein. Location. Protein structure. Protein molecule shapes. Protein is a reserve substance. Protein structure. Properties of protein (experience). Qualitative reaction to proteins. Functions of protein. Construction Catalytic. Regulatory. Motor. Transport. Protective. Energy. Without proteins, the growth of plants, animals and humans is impossible. Proteins are found in: Meat. Fish. Gribakh. Bobovykh. The protein molecule consists of 20 amino acids, which alternate in various ways. “*” 10 of which are irreplaceable and must be supplied with plant and animal foods. - Squirrels.ppt

Squirrels lesson

Squirrels. Protein content in the body (as a percentage of dry weight). Structure of a protein molecule. Qualitative reactions. Biuret Xanthoprotein HNO3 NaOH CuSO4. Quaternary structure of a protein molecule. General properties of proteins. Functions of proteins. What is life? Protein content in food. - Squirrels lesson.pps

Protein biology

Lesson topic: “proteins are biopolymers of life.” Squirrels. Life is a way of existence of protein bodies.” Composition of proteins Common amino acids that make up proteins. Alanin. Arginine. Asparagine. Aspartic acid. Phenylalanine. Histidine. Glycine. Glutamine. Glutamic acid. Isoleucine. Leucine. Lysine. Methionine. Proline. Serin. Tyrosine. Threonine. Tryptophan. Cysteine. Valin. Protein composition. Fig.1 Optical isomerism alanine Rice. 2 Peptide bonds in the protein structure. Fragment of the chain of normal hemoglobin: –glu-glu-lys-. Fragment of the chain of abnormal hemoglobin: -val-glu-lys-. Structure of proteins. Protein conformation is the spatial configuration of a protein molecule, a special geometric shape. - Protein biology.pptx

Proteins substance

Organic substances of the cell PROTEINS. Proteins are the main components of the cell. Chemical composition proteins. Protein monomers are amino acids. amino acid – organic matter, which simultaneously contains an amino group and a carboxyl group. There are 20 known amino acids from which proteins are built. General formula AK: All AKs differ in their radicals. In protein, amino acids are linked together by peptide bonds (NH-CO) to form polypeptide chains. Functions of proteins. Enzymatic Construction Transport Contractile Regulatory Food Protective Energy Receptor. Enzyme proteins. Accelerators of biochemical reactions in the cell. (lipase, amylase, pepsin). - Protein substance.pptx

Organic matter proteins

Squirrels. Food. Foods containing proteins. Protein composition. The mode of existence of protein bodies. Amino acids. Classification of proteins. Levels of organization of a protein molecule. Protein structures. Twisted spiral shape. Protein denaturation. Functions of protein. Structural function. Enzymes. Regulatory proteins. Protective proteins. Transport proteins. Motor proteins. Receptors. Storage proteins. - Organic matter proteins.ppt

Properties of proteins

Primary structure of a protein. Peptide group. Peptide bond. A secondary structure helix held together by hydrogen bonds. Tertiary structure - a coil of secondary structures, held together by S - S and S - H bonds. QUARTERNARY STRUCTURE - a complex of tertiary structures (an example of a hemoglobin molecule). Denaturation. Renaturation. Study of the properties of proteins. Protein solubility. Protein chicken egg partially soluble. Conducting a lesson. Study of the influence of substances on protein structure. Alcohol + protein = sediment (denaturation). Protein + heavy metal salt (CuSO4) = precipitate (denaturation). Heating the protein leads to denaturation. - Properties of proteins.ppt

Protein structure

The structure of proteins. Examination homework. Terminological work. Hydrophobes. Macroelements. Hydrophiles. Buffering. Polysaccharides. Lipoproteins. Over 170 different amino acids are found in cells and tissues. The structure of proteins is the primary structure. Protein structure is secondary structure. Typically, a protein molecule resembles an extended spring. Protein structure is tertiary structure. Most proteins have polypeptide chains folded in a special way into a compact globule. The way the polypeptide chains of globular proteins fold is called tertiary structure. The protein structure is quaternary structure. - Structure of proteins.ppt

Protein molecule structure

Squirrels. Antoine Francois de Fourcroix. Structure of proteins. A three-dimensional structure is formed as a result of the interaction of structures at lower levels. There are four levels of protein structure. Primary structure. The primary structure consists of amino acid residues repeated in strict sequence. Secondary structure of protein. Tertiary structure of a protein. Quaternary structure of protein. Subunit structure of a protein. The relative arrangement of several polypeptide chains as part of a single protein complex. The importance of protein for living organisms. Proteins carry out metabolism and energy transformations. - Structure of a protein molecule.ppt

Functions of proteins

Topic: “Properties and functions of proteins.” Objectives: Study the properties and functions of proteins. There are acidic, basic and neutral proteins. There are proteins that are unusually chemically active (enzymes), and there are those that are chemically inactive. There are resistant to various conditions external environment and extremely unstable. 1. Properties of proteins. The cause of denaturation is the breaking of bonds that stabilize a certain protein structure. What proteins are called acidic? Proteins that contain more acidic amino acids lower the pH. What proteins are called neutral? Proteins that have the same number of carboxyl and amino groups. - Functions of proteins.ppt

Proteins and their functions

Protein structure and functions. Concept of proteins. Functions of protein. The functions of proteins are extremely diverse. Construction material. proteins are involved in the formation of the cell membrane, organelles and cell membranes. Built from proteins blood vessels, tendons, hair. Transport function of proteins. Catalytic role. all cellular catalysts are proteins (active centers of the enzyme). Protective function. Production of protein bodies and antibodies to neutralize foreign substances. Energy function. 1 g of protein is equivalent to 17.6 kJ. Motor function. Contractile proteins cause all movement. - Proteins and their functions.ppt

Amino acids and proteins

Proteins and amino acids. Squirrels. With the help of proteins we digest food and fight diseases. Biological "beads". The protein molecule is very long. This is how beads are strung onto a thread into a necklace. In polymers, the role of a thread is played by chemical bonds between bead molecules. For example, red people are attracted to yellow people. Something similar happens in proteins. Energy value of some products. Amino acid structure. Each amino acid molecule has a carbon atom bonded to four substituents. Amino acids. For normal functioning, the body needs a full set of 20 basic a-Z-amino acids. -

How is it formed

protein molecule?

Protein - sequence of amino acids,

linked to each other by peptide bonds.

Functions of proteins:

1. Structural (plastic). Proteins form all cellular structures.

Keratin is the main component of hair, nails, horns, and hooves.

2. Enzyme proteins.

Amylase - converts starch into glucose.

DNA polymerase I – participates in the repair of DNA molecules.

3. Proteins-hormones. 50% of human hormones are proteins. Insulin regulates glucose consumption, vasopressin stimulates the reabsorption of water by the kidneys.

4. Transport function. Hemoglobin- carries oxygenserum albumintransports fatty acids transferrin - iron transport.

5. Reserve (energy)– examples: egg albumin, muscle protein, lymphoid organs, epithelial tissue and liver.

6. Receptor. By using receptor proteins binding of various bioregulators (hormones, mediators, biogenic amines...) occurs.

7. Contractile. Actin, myosin

Participate in muscle contraction.

8. Immunological. Antibody formation.

9. Hemostatic. Blood clotting proteins.

10. Neutralizing. Milk proteins are an antidote for salt poisoning heavy metals(lead, copper, zinc...)

11. Creation of biopotentials

cell membranes and mitochondrial membranes.

12. Gene regulatoryfunction - protein biosynthesis in the cell.

13. Proteins are buffer systems.

14. Proteins are toxins (insect poisons...)

How is a protein molecule formed?

The spatial structure of proteins has 4 levels of organization.

Primary structure is the sequence of amino acid residues in a polypeptide chain. Formed by peptide bonds. (Type of bond – covalent).

The base of the chain is CO-CH-NH-. Radicals located outside the chain carry the main burden when proteins perform their functions.

Secondary structure squirrel. At the level of secondary structure, protein “beads” can be arranged in the form of a spiral and in the form of a folded layer.

Secondary stacking occurs only due to hydrogen bonds –N-H......O=C-

Two chain laying options:

Alpha helix (alpha structure). It is right-handed and is formed by hydrogen bonds between peptide groups of amino acid residues.

Beta fold layer – protein the molecule lies like a snake. Connection-

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“Wherever we find life, we find it associated with some proteinaceous body, and wherever we find any proteinaceous body that is not in the process of decomposition, we, without exception, encounter the phenomenon of life.” (K. Marx, F. Engels. Collected Works. T.20).

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Antoine Francois de Fourcroix

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Proteins are complex high-molecular natural compounds built from α - amino acid residues connected by peptide (amide) bonds - CO - NH -.

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The number of amino acid residues included in protein molecules is different: in insulin there are 51 (20 in one and 31 in the other chain), in myoglobin - 140. The molecular weights of proteins can range from 10,000 to several million.

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Mr(egg white) = 36,000; Mr(muscle protein) = 1,500,000. The composition of hemoglobin is expressed by the formula (C738H1166O208N203S2Fe)4

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The composition of proteins includes: C – 50 – 52%; N – 6 – 8%; O – 19 – 24%; N – 15 – 18%; S – 0.5 – 2.0%.

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Structures of a protein molecule

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Different ways to depict the three-dimensional structure of a protein

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Chemical properties:

hydrolysis (when heated with solutions of acids, alkalis, under the action of enzymes) Protein ↔ amino acids → blood into all cells and tissues of the body

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OH O H IIII I H2N─CH2 ─C ─N ─CH─C─N ─CH─C=O → H2OI H2OI I CH2 CH2 OH I I tripeptide OH SH → H2N─CH2 ─C=O + H2N─CH─C=O + H2N─CH─C=O I I III OH CH2 OHCH2 OH I I OHSH glycine serine cysteine

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2) denaturation - disruption of the natural structure of the protein (under the influence of heat and chemical reagents)

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3) amphotericity: + NaOH __________ properties of acids Protein __________ properties of bases + HCl

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4) color reactions of proteins - qualitative reactions a) xanthoprotein reaction: Protein +HNO3 conc. → yellow color b) biuret reaction: Protein + Cu(OH)2↓ → violet solution 5) combustion - the smell of burnt feathers

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The role of proteins in the cell: 1. Building material for the shell, organelles and membranes of the cell. Blood vessels, tendons, and hair are built from them. 2. Catalytic function. All cellular catalysts are proteins. 3. Motor function. Contractile proteins cause all movement.

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4. Transport role - the blood protein hemoglobin attaches oxygen and distributes it to all tissues. 5. Protective function - the production of protein bodies of antibodies to neutralize foreign substances. 6. Energy function - the decomposition of 1 g of protein releases 17.6 kJ of energy.

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Protein content in various human tissues

In muscles – up to 80%; in the spleen, blood, lungs - about 72%; in the skin – 63%; in the liver – 57%; in the brain – 15%; adipose tissue, bone and dental tissue contain from 14 to 28% proteins.

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Protein synthesis

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According to the World Health Organization, approximately half of the world's population is in a state of protein starvation, and the global shortage of dietary protein is about 15 million tons per year, with the protein intake per day for an adult being 115 grams

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check yourself

1. The main carrier of life are… 2. … are complex high-molecular compounds built from…. 3. Elemental composition of proteins: ... . 4. The molecular weight of proteins varies from ... to ....