How is formed
protein molecule?
Amino acid sequence protein
associated with each other peptide bonds.
Protein features:
1. Structural (plastic). Proteins form all cellular structures.
Keratin - main component Hair, nails, horns, hoofs.
2. Proteins-enzymes.
Amylaza - turns starch in glucose.
DNA polymerase I - participates in reparation DNA molecules.
3. Proteins hormones. 50% of human hormones - protein. Insulin - regulates glucose consumption, Vasopressin - stimulates the reverse water absorption by the kidneys.
4. Transport function. Hemoglobin- transfers oxygenserum albumintransfers fatty acidstransfrine-transport of iron.
5. Backup (energy)- Examples: egg albumin, muscle protein, lymphoid organs, epithelial tissue and liver.
6. Receptor. Via protein receptorsthere is a binding of various bioregulators (hormones, mediators, biogenic amines ...).
7. Cutting. Aktin, Mozin.
Participate in the contraction of the muscles.
8. Immunological.The formation of antibodies.
9. Hemostatic. Blood coagulation proteins.
10. Nequance. Milk proteins are antidote in poisoning salts of heavy metals (lead, copper, zinc ...)
11. Creation of biopotentials
membranes of cells and membranes mitochondria.
12. Gennoregulatoryfunction - biosynthesis protein in the cell.
13. Belky-buffer systems.
14. Proteins - toxins (insect poisons ...)
How is the protein molecule formed?
In the spatial structure of proteins - 4 levels of the organization.
Primary structure-sequence of amino acid residues in the polypeptide chain. It is formed due to peptide bonds. (Type of communication - translation).
The base of the chain is-CH-NH-. Radicals are located outside the circuit carry the main load when performing their functions with proteins.
Secondary structuresquirrel. At the level of the secondary structure, protein "beads" can fit in the form of a spiral and in the form of a folded layer.
Secondary styling occurs only due to hydrogen bonds -N-H ...... O \u003d C-
Two chain laying options:
Alpha spiral (alpha structure). It is human rights, formed using hydrogen bonds between peptide groups of amino acid residues.
Beta-folded layer -Belk The molecule is a snake. Communication
Description of the presentation on individual slides:
1 Slide
Slide description:
Proteins Objectives: give definition to learn the composition to study the spatial structure to learn the basic functions of proteins to study the classification to learn properties
2 Slide
Slide description:
The exceptional protein property is self-organization of the structure, i.e. Its ability to spontaneously create a certain spatial structure inherent in this protein. Essentially, all the activities of the body (development, movement, the performance of various functions and much more) is associated with protein substances. Without proteins it is impossible to imagine life.
3 Slide
Slide description:
Proteins - high molecular weight natural compounds (biopolymers) consisting of amino acid residues that are connected by peptide bond. Proteins proteins proteins
4 Slide
Slide description:
The composition of protein substances includes: carbon, hydrogen, oxygen, nitrogen, sulfur, phosphorus. Hemoglobin - C3032H4816O872N780S8FE4. The molecular weight of proteins ranges from several thousand to several million. MR Squirrel Eggs \u003d 36 000, MR Muscle protein \u003d 1 500,000 Water - 65% Fats - 10% proteins - 18% Carbohydrates - 5% Other inorganic and organic substances - 2% Qualitative composition Belkov
5 Slide
Slide description:
The structure in the molecules of the protein α - amino acids are interconnected by peptide (-so-nh-) connections about the o o r1 R2 R3 constructed polypeptide chains or individual sections inside the polypeptide chain may be some cases Advanced interconnected disulfide (-S-S-) connections, or, as they are often called disulfide bridges
6 Slide
Slide description:
The primary structure is the sequence of alternation of amino acid residues in the polypeptide chain. The sequence of compounding the amino acid residues in the polypeptide chain was called the primary protein structure. Total number Different types of proteins in all types of living organisms is 1010-1012
7 Slide
Slide description:
The secondary structure is the spatial configuration of the polypeptide chain, that is, its possible location in space. For proteins, the most common variant of the secondary structure is a spiral. The secondary structure has most of the proteins, however, not always on all over the polypeptide chain.
8 Slide
Slide description:
The tertiary structure is a three-dimensional configuration that the swirling spiral takes place in space. The tertiary structure explains the specificity of the protein molecule and its biological activity. In the formation of a tertiary structure, in addition to hydrogen bonds, ionic and hydrophobic interaction plays a major role. According to the characters of "packaging", the protein molecule distinguish globular, or spherical, and fibrillary, or filamentine, proteins.
9 Slide
Slide description:
The quaternary structure is the location in the space of several polypeptide chains, each of which has its primary, secondary and tertiary structure and is called the subunit. In some cases, individual protein subunits with hydrogen bonds, electrostatic and other interactions form complex ensembles. In this case, a quaternary structure of proteins is formed.
10 Slide
Slide description:
Classification There are several protein classifications. They are based on different signs: the degree of complexity (simple and complex); Molecules shape (globular and fibrillar proteins); Solubility in individual solvents (water-soluble, soluble in dilute saline solutions - albumin, alcoholoisseable - prolaminones, soluble in diluted alkalis and acids - vulnery); Function performed (for example, spare proteins, skeletal, etc.).
11 Slide
Slide description:
The functions of proteins construction (plastic) - proteins are involved in the formation of a cage shell, organoids and cell membranes. Catalytic - all cell catalysts - proteins (active enzyme centers). Motor - contracting proteins cause any movement. Transport - blood protein hemoglobin joins oxygen and distribute it in all tissues. Protective - Development of protein bodies and antibodies to neutralize alien substances. Energy - 1 g of protein is equivalent to 17.6 kJ. Receptor - reaction to an external stimulus
12 Slide
Slide description:
Chemical properties proteins proteins - amphoteric electrolytes. With a certain value of the pH of the medium (it is called an isoelectric point) the number of positive and negative charges In the protein molecule equally. This is one of the properties of a protein. Proteins at this point are either either, and their solubility in water is the smallest. The ability of proteins to reduce the solubility when the electrophetrality is reached, their molecules is used to release them from solutions, for example, in the technology of obtaining protein products.
13 Slide
Slide description:
1. Hydrolysis (acid-main, enzymatic), as a result of which amino acids are formed. 2. Denaturation is a violation of the natural structure of the protein under the action of heating or chemical reagents. The denatured protein loses its biological properties. Chemical properties of proteins The primary protein structure during denaturation is preserved. Denaturation can be reversible (so-called, renault) and irreversible. An example of irreversible denaturation with thermal exposure is the coagulation of egg albumin when cooking eggs.
14 Slide
Slide 2.
"Everywhere, where we meet life, we find that it is connected with any protein body, and everywhere, where we meet any protein body that are not in the process of decomposition, we meet and have a phenomenon of life without exception." (K. Marx, F. Enteps. Collected Works. T.20).
Slide 3.
Antoine Francois de Furkrua
Slide 4.
Proteins are complex high molecular weight natural compounds constructed from α-amino acid residues connected by peptide (amide) bonds - NH -.
Slide 5.
The number of amino acid residues included in the protein molecules is different: in insulin of their 51 (20 in one and 31 - in another chain), in myoglobin - 140. The molecular masses of proteins can range from 10,000 to several million.
Slide 6.
Mr (Eggs protein) \u003d 36,000; Mr (muscle protein) \u003d 1 500 000. The composition of hemoglobin is expressed by the formula (C738H1166O208N203S2FE) 4
Slide 7.
The protein includes: C - 50 - 52%; N - 6 - 8%; O - 19 - 24%; N - 15 - 18%; S - 0.5 - 2.0%.
Slide 8.
Structures of a protein molecule
Slide 9.
Different ways of image of the three-dimensional protein structure
Slide 10.
Chemical properties:
hydrolysis (when heated with acid solutions, alkalis, under the action of enzymes), a protein ↔ amino acids → Blood in all cells and tissues of the body
Slide 11.
OH OH IIII I H2N─CH2 ─C ─n ─ch─c─ ─ch─c \u003d O → H2OI H2OI I CH2 CH2 OH II Tripeptide OH SH → H2N─CH2 ─C \u003d O + H2N─CH─C \u003d O + H2N─ch─c \u003d OII III OH CH2 OHCH2 OH II OHSH Glicin Serine Cysteine
Slide 12.
2) Denaturation - violation of the natural structure of the protein (under the action of heating and chemical reagents)
Slide 13.
3) amphoterity: + NaOH __________ Society of protein acids __________ Base properties + HCl
Slide 14.
4) Color reactions of proteins - high-quality reactions A) Xanthoprotein reaction: protein + HNO3 conc. → Yellow staining b) buret reaction: protein + Cu (OH) 2 ↓ → Solution of purple color 5) burning - smell of burning feathers
Slide 15.
The role of proteins in a cage: 1. Construction material Common, organoids and cell membranes. Of these, blood vessels, tendons, hair were built. 2. Catalytic function. All cell catalysts are proteins. 3. Motor function. Cutting proteins cause any movement.
Slide 16.
4. Transport role - hemoglobin blood protein joins oxygen and spreads over all tissues. 5. Protective function - the production of protein bodies of antibodies to neutralize alien substances. 6. Energy function - with decomposition of 1 g of protein, 17.6 kJ of energy is distinguished.
Slide 17.
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%; Fat fabric, bone and teeth tissue contain from 14 to 28% proteins.
Slide 18.
Synthesis proteins
Slide 19.
According to the World Health Organization approximately half of the population globe It is in a state of protein starvation, and the global shortage of the food protein is about 15 million tons per year with the norm of protein consumption per day with an adult man 115 grams
Slide 20.
check yourself
1. The main carrier of life is ... 2. ... - These are complex high molecular compounds built from .... 3. The elemental composition of proteins: .... 4. The molecular weight of proteins varies from ... to ....
Slide 1.
Slide 2.
Proteins (proteins) are the basis of life. They are animal and vegetable origin. Animal proteins are contained in meat, fish, seafood, bird, dairy products, eggs. The ratio contained in them amino acids is closest to the optimal for the human body. Vegetable proteins are contained in legume crops, nuts, algae, chocolate, potatoes, various cereals. The human body needs both animals and vegetable proteins: they mutually complement each other. The total daily need of the body in proteins is about 20% of the diet. What is protein? Proteins are a key part of each human body cell. They represent high molecular weight biological compounds and serve as a "building material", from which the body's tissues are built: muscles, skin, as well as hair and nails. They make it possible all the main manifestations of life: digestion, metabolism, the ability to increase, irritate fabrics, reproduction and even the highest form of motion of matter - thinking. The lack of protein in the nutrition of the child can lead to a sharp lag of its development, and in adults decreases the body's resistance to colds and infectious diseases, disability falls. The word "protein" comes from the Greek word "Proteios", which means "occupying first". So this gives us a good idea of \u200b\u200bthe importance of protein in nutrition!
Slide 3.
General formula amino acids. The amino group has the properties of the base. The group radical - different in all carboxyl group has acid properties between the combined amino acids, a peptide bond arises, on the basis of which the compound polypeptide is formed.
Slide 4.
Slide 5.
Structure of protein molecule
Primary, linear, in the form of a polypeptide chain: secondary due to hydrogen bonds: spiral-, in the form of harmonica-.
Slide 6.
Tertiary, globular, due to hydrophobic interactions. Quaternary- combining several molecules with a tertiary structure.
Slide 7.
Properties of protein.
First, proteins are predominantly water-soluble molecules and, therefore, can exhibit their functional activity only in aqueous solutions. Secondly, protein molecules carry a large superficial charge. Thirdly, proteins are thermolabile, i.e. Show their activity in the narrow temperature framework.
Slide 8.
Denaturation - loss by a protein molecule of its structural organization. The effect of increased temperature, dehydration, changing the pH and other effects cause the destruction of the structural organization of proteins.
Slide 9.
Renaturation is the restoration of the lost structure. If the change in the conditions of the medium does not lead to the destruction of the primary structure of the molecule, then the structure of the protein and its functional activity is completely recreated when restoring normal conditions of the medium.
Slide 10.
Hormones: hormones - proteins that are produced by alive cells. The hormones are circulated in body fluids, such as blood, and causes a certain effect on other cells, which, as a rule, at some distance from the place where the hormone is produced. For example: Adrenaline is a hormone, which is produced by the body during stress and leads to accelerating the frequency of heart abbreviations and respiration. Enzymes: They are complex proteins formed in plant and animal cells, and contribute to the transformation of one substances (substrates) to other (products). Digestive enzymes, for example, help our body recycle food into chemicals that can be absorbed into blood. Antibodies: Antibodies - protein produced by white blood cells in response to an alien substance called an antigen, such as bacteria and viruses. Hormones, enzymes and antibodies are just some of the substances that, ultimately, are formed in the organism of protein food.
Slide 11.
Protein functions. Plastic Function: Proteins are involved in the formation of all cell membranes and cell organoids, as well as extracellular structures. Catalytic role of proteins.
Slide 12.
Motor function - contracting proteins. These proteins participate in all types of movement to which cells and organisms are capable of: the flickering of the cilia and the beating of flavors from the simplest, cutting muscles in multicellular animals, the movement of the leaves in plants.
Slide 13.
Transport function of proteins: the addition of chemical elements, biologically active substances. Special transport proteins move RNA. Protective function - antibody. Energy function - with a full splitting of 1 g of protein to final products, 17.6 kJ of energy is highlighted. Hormonal, or receptor-proteins are part of many hormones, take part in the regulation of vital processes.
Slide 14.
Daily protein needs The required amount of protein per day depends on various factors, including the floor, age and level of physical activity. They must be about 20% of the daily nutritional need. Lack of proteins in a daily diet reduces immunity and contributes to the development of various diseases, including cancer. You can significantly increase immunity if you add 15 g of dairy proteins to a daily rate of 1 g / kg (cheese). Proteins are rarely used to produce energy. This is the work of carbohydrates and fats.
Structure of protein
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