Presentation on the topic of proteins in chemistry.

Proteins, or protein substances, are called high molecular weight (molecular weight varies from 5-10 thousand to 1 million or more) natural polymers, whose molecules are constructed from amino acid residues connected by amide (peptide) bond. catalytic (enzymes); regulatory (hormones); structural (collagen, fibroin); Motor (MIOSIN); transport (hemoglobin, mioglobin); protective (immunoglobulins, interferon); Spare (casein, albumin, glyadin). Among the proteins there are antibiotics and substances that have toxic effects. Proteins - the base of the biomembrane, the most important component of the cell and cellular components. They play a key role in cell life, leaving the material basis of its chemical activities. 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. Proteins are the most important component of the food of man and animals, the supplier of the amino acids you need. Water - 65% Fats - 10% proteins - 18% Carbohydrates - 5% Other inorganic and organic substances - 2% In protein molecules α - amino acids are interconnected by peptide (-so-NH-) connections ... N CH CN CH CN CH CN CH C ... HR O H R1 O H R2 O H R3 O constructed by the polypeptide chains or individual sections inside the polypeptide chain may be additionally related to disulfide (-ss-) connections, or, as they The ionic (salt) and hydrogen bonds, as well as hydrophobic interaction, and hydrophobic interaction are a large role in the creation of proteins, and hydrophobic interaction - a special type of contact between the hydrophobic components of protein molecules in the aqueous medium. All these bonds have different strength and ensure the formation of a complex, large protein molecule. Despite the difference in the structure and functions of protein substances, their elemental composition varies slightly (in% per dry weight): carbon-51-53; oxygen-21.5-23.5; nitrogen-16.8-18.4; hydrogen-6.5-7.3; Sulfur-0.3-2.5 Some proteins contain phosphorus, selenium and other elements in small quantities. The sequence of compounding the amino acid residues in the polypeptide chain was called the primary protein structure. The total number of different types of proteins in all types of living organisms is 1010-1012, most of the proteins have a secondary structure, however, not always on all over the polypeptide chain. Polypeptide chains with a specific secondary structure can be located differently in space. This spatial location was called the tertiary structure. 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. 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. However, it should be noted once again that in the organization of higher protein structures, an exceptional role belongs to the primary structure. Protein molecule structure The tangle is a floccular structure of disulfide and ionic communications CO ... HNCO ... HN 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); Performed skeletal, etc.). Function (for example, spare 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 is the same. This is one of the properties of the protein. Proteins at this point are either-erased, and their solubility in water The smallest. The ability of proteins to reduce the solubility when the electrophetrality is reached, their molecules are used to release them from solutions, for example, in the technology of obtaining protein products. The hydration process means binding to water proteins, while they exhibit hydrophilic properties: swell, their mass and volume increase. Squirrel Its partial dissolution. The hydrophilicity of individual proteins depends on their structure. The hydrophilic amide (co-NH-, peptide bond), amine (NH2) and carboxyl (coxy) of the group attract the water molecules in the composition and located on the surface of the protein macromolecule Orienting them on the surface of the milk Ul. The surrounding protein globes hydrate (aqueous) shell prevents aggregation and precipitation, and therefore contributes to the stability of the protein solution. With limited swelling, concentrated protein solutions form complex systems, called jets. The student is not fluid, elags, possess plasticity defined by mechanical strength, are able to maintain their shape. Globular proteins can be completely hydrated, dissolving in water (for example, milk proteins), forming solutions with low concentration. The hydrophilicity of grain and flour proteins plays a major role when storing and processing grain, in bread maker. The dough, which is obtained in bakery production, is a swelling protein in water, a concentrated jelly containing the starch gram. At denaturation, under the influence of external factors (temperature, mechanical effects, the actions of chemical agents and a number of other factors), there is a change in the secondary, tertiary and quaternary structures of the protein macromolecule, that is, its native spatial structure. Primary structure, and therefore. And the chemical composition of the protein does not change. Physical properties change: the solubility is reduced, the ability to hydration is lost, biological activity is lost. The shape of the protein macromolecule is changing, aggregation occurs. At the same time, the activity of some chemical groups increases, facilitates the effects of proteolytic enzyme proteins, and therefore it is easier to hydrolyze. In the food technology, thermal denaturation of proteins is of particular practical importance, the degree of which depends on the temperature, the duration of heating and humidity. Denaturation of proteins can be called and mechanically exposed (pressure, rubbing, shaking, ultrasound). Finally, the denaturation of proteins leads the effect of chemical reagents (acids, alkalis, alcohol, acetone. All these techniques are widely used in the food industry and biotechnology. Under the process of foaming, the ability of proteins to form high-concentrated liquid-gas systems, called foams, is a foam stability in which the protein is a foaming agent depends not only on its nature and on the concentration, but also on temperature. Proteins as foaming agents are used in the confectionery industry (grazing, marshmallow, souffle). The structure of the foam has bread, and this affects its taste properties. . For the food industry, two very two very important process can be distinguished: 1) proteins hydrolysis under the action of enzymes; 2) the interaction of amino groups of proteins or amino acids with carbonyl groups of restoring sugars. The speed of the hydrolysis of the protein depends on its composition, molecular structure, enzyme activity and conditions. The reaction of hydrolysis with the formation of amino acids in a general form can be written as: proteins are lit with the formation of nitrogen, carbon dioxide and water, as well as some other substances. The burning is accompanied by a characteristic smell of burning feathers. The following reactions are used: xanthoprotein, at which the interaction of aromatic and heteroatomic cycles in the protein molecule with concentrated nitric acid, accompanied by the appearance of yellow color; Buret, in which the interaction of sloping proteins with a solution of copper (II) sulfate solution with the formation of complex compounds between Cu2 + ions and polypeptides. The reaction is accompanied by the appearance of purple painting.

Proteins

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Proteins. From the history. Term. The size of the protein can be measured in the number of amino acids or in Dallands. Simple squirrels. Sophisticated proteins. Protein functions. Organization levels. Primary structure. Secondary structure. Tertiary structure. Quaternary structure. Types of protein structure. Globular proteins. Fibrillar proteins. Denaturation. - Proteins.pptx

Lesson protein

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Proteins. The birth of the lesson begins: the tasks of the lesson: to form knowledge about the chemical properties of proteins. Learn to confirm the chemical properties of proteins experimentally. Objectives of the lesson: Developing: Development of ability to analyze, compare, draw conclusions about protein properties. Lesson plan. Type of lesson: lecture with interview elements. The lesson method: explanatory-stimulating. Type of lesson: lesson learning new knowledge based on already available. Intergovernmental ties: biology, nutritional physiology. Logistics lesson: CD disk "Protein structure". Chemistry textbook 11 class (G. Rudzitis, F.G. Feldman). - List of protein.ppt

Chemistry proteins

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Proteins. Content. Definition. Protein functions. The skin and hair protect the inner medium of the body from external influences. The composition of mucus and synovial fluid includes mucoproteins. Sources of amino acids. Such amino acids are called indispensable. Amino acids involved in the creation of proteins. Glycine Alanin Valin Leucin Isoleucin Serin Thinonin Cysteine. Metionine Lizin Arginine Asparagin Asparaginic acid glutamic acid. Glutamine Phenylalanin Tyrosine Triptophan Gistidin Proline. The structure of the polypeptide chain. Sequential compound of amino acids in the formation of a protein molecule. - Chemistry proteins.ppt.

Amino acids

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Amino acids. Like many biomolecules, amino acids exist in the form of mirror isomers (stereoisomers). Usually, only L-isomers of amino acids participate in biological processes. The concept of amino acids. Amino acids - compounds, in the molecules of which are at the same time there are amino and carboxyl groups. Classification of amino acids. ? -Mic acidic acid. ? -Mic acidic acid. ? -Mic acidic acid. Glycine, monoaminomocarboxylic acid. Aspartic acid, monoaminodicarboxylic acid. Lysine, diaminonocarboxylic acid. Neutral hydrophobic amino acids. Isoleucine. - amino acids.ppt.

"Amino acids" chemistry

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Amino acids. General formula. Biological role. Amino acid nomenclature. Diaminohexanic acid. Isomerius of the carbon skeleton. Properties. Methods for obtaining. The formation of polypeptides. Getting amino acids. Natural amino acids. Amino acid application. Organic connections. Make a formula. - "Amino acids" chemistry.ppt

Basic amino acids

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Amino acids. Definition of amino acids. The sequence of studying a new topic. The word "amino acids" in terms of word formation. Offer the general formula for amino acids. Radical. Connections. Aminoacetic acid. Aminopropionic acid. Aminicarian acid. Isomerius of carbon skeleton amino acids. Isomerization of the position of the amino group. Formulas. Glycine. Physical properties of AK. Getting amino acids. Amino group. Neutral reaction of glycine solution. Alkaline medium. Acid character. AK reactions. Interaction with the grounds. Interact with the main oxides. Creative task. - Basic amino acids.pptx

Amino acid properties

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Amino acids. NH2 - CH - COOH | R. Derivatives of carboxylic acids, in which atom n in the radical is substituted on the amino group. CH3COs Acetic Acid H - CH - Soam Aminoacetic Acid | NH2. (Glycine). Physical properties. Chemical properties. 1806 Rafael Piria Hydrolysis Asparagina Asparagic acid But-C-CH2-CH-coo? | About NH2. 1909 K. Ikyda Dried algae - enhance the flavor and taste of food - nutritional supplements. (Alanine). - Properties of amino acids.ppt.

Types of amino acids

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Chemical nature protein. Proteined amino acids are? -Cheel organic acids. The general formula of amino acids. Brief symbols of amino acids. Classification for physiological attribute. Classification in chemical nature. Glycine. The central link of purine bases. Glycine is a lot in fibrillar proteins, gelatin, fibrillar connections silk, hair. Participates in the synthesis of threonine, applied in pharmacy. Alanine. Alanine easily turns into a liver in glucose and vice versa. Valin. Valin is an indispensable amino acid. Leucine. Leucine (? -Aminoisocapronic acid) is an aliphatic amino acid; An indispensable amino acid. - types of amino acids.ppt.

Amino acids proteins

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Amino acids. Proteins. Lesson plan. The composition and properties of amino acids. Amphoteriness amino acids. Polycondensation reaction. Chemical properties of proteins. 1. The present and properties of amino acids. Glycine is a colorless crystalline substance, well soluble in water, sweetish taste. Glycine plays a big role in metabolism. Used as a drug to improve cerebral circulation. 2. Amino acid amphoteriness. Glycinate potassium. Glicin chloride salt. 3. Polycondensation reaction. 4. Squirrels. Proteins-products of the reaction of polycondensation of amino acids. Proteins have a very complex structure. - amino acids proteins.ppt.

Amino acids and proteins

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Amino acids and proteins. Building, properties. Amino acids. Indispensable amino acids. Acid and basic properties. Non-ionic form; Idealized amino acid. Zwitter-ion; Amino acid in solid state. Isoelectric point (PI). Methods for producing amino acids ammination? -Galo-substituted acids. Methods for producing amino acids bromination with malonic acid. Methods for producing amino acids Synthesis of Strakker-Zelinsky. Methods for producing amino acids. Methods for producing amino acids The biological method of obtaining amino acids. Food with adding a racemic mixture A-amino acids. - amino acids and proteins.ppt

"Amino acids and proteins" chemistry

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Amino acids, proteins. Amino acids. Properties of amino acids. Amino acid names. The formation of peptide communications. Peptide Communication Education Scheme. Amino acids are necessary for protein synthesis in living organisms. Protein is a high molecular weight organic compound. The protein includes chemical elements. In physical properties, proteins are divided. Proteins are components of hair. Insulin molecule. Structure of protein. The secondary structure - arises by twisting primary. The tertiary structure is a globular form. Quaternary structure. Complex of four macromolecules. - "Amino acids and proteins" chemistry.pptx

"Amino acids and proteins" Chemistry 10 class

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Amino acids. Plan characteristics. Organic connections. Derivatives of carboxylic acids. Heterofunctional (bifunctional) compounds. General formula. Classification. C - SO - Son. Lysine. Isomeria. In living organisms. Physical properties. Chemical properties. Ethyl ether. Chloride salt. Water solubility. Polypeptide. Peptide connection. Dipepidid. Methods for obtaining. Louis Voklen. Natural amino acids. Dried algae. Proteins. High molecular weight organic compounds. Hydrogen. The main structural components of proteins are amino acids. - "Amino acids and proteins" Chemistry grade 10.pptx

Physico-chemical analysis

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Multidimensional physico-chemical analysis. The content of the report. GK Andersen. Physico-chemical analysis. One-dimensional physico-chemical analysis. Model of multidimensional physico-chemical analysis. MFCA Toolkit. Factor analysis of the properties of the glycine solution. Factor analysis. Chemical reactions in solution. Diagrams of ional forms. Reaction. Experiment. Dispersion analysis. Dependent variable. Refraction ratio. Three-dimensional thermal conductivity diagram. Regression analysis. Simulation of the latent structure. Model of the covariance structure. Frame diagram. Modeling results. -

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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

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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.

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Proteins - high molecular weight natural compounds (biopolymers) consisting of amino acid residues that are connected by peptide bond. Proteins proteins proteins

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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 of proteins

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The structure in the α - amino acid protein molecules are interconnected by peptide (-so-nh-) connections about R R1 R2 R3, thus constructed polypeptide chains or individual sections inside the polypeptide chain may be additionally interconnected by disulfide (- SS-) connections, or, as they are often called disulfide bridges

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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. The total number of different types of proteins in all types of living organisms is 1010-1012

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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.

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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.

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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.

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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.).

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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

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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 is equally. This is one of the properties of the 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.

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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.

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