Functions of proteins in the human body presentation. The structure and functions of proteins
Presentation on the topic: Proteins. Properties and functions of proteins in the body
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Presentation on the topic: Squirrels. Properties and functions of proteins in the body
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Introduction I. History of protein discovery II. Structure of proteins. Structure of proteins; Spatial structure; Properties of proteins; III. Functions of proteins. IV. Practical work.Protein denaturation;Proof of the functioning of proteins as biocatalystsColor reactions for proteinsV. Conclusion. VI. Literature.
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Proteins are natural organic compounds, which provide all the life processes of any organism. “Life is a way of existence of protein bodies.” Based on the achievements of contemporary natural science, F. Engels laid the scientific philosophical and theoretical foundations for ideas about life and protein as its most essential “carrier” and “ determinant". The correctness of the theory of F. Engels is fully confirmed by modern biological chemistry, molecular biology and biophysics, which have more versatile experimental data, both about chemical structure proteins, and their role and importance in life.
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Squirrels got their name from egg white, which has been used by man since time immemorial as an integral part of food. According to the descriptions of Pliny the Elder, already in Ancient Rome egg white was also used as a remedy. However, the true history of protein substances begins when the first information about the properties of proteins appears as chemical compounds(clotting when heated, decomposition by acids and strong alkalis, etc.).
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To early XIX century, the first works on the chemical study of proteins appear. Already in 1803, J. Dalton gives the first formulas of proteins - albumin and gelatin - as substances containing nitrogen. In 1810, J. Gay-Lussac conducts chemical analyzes of proteins - blood fibrin, casein and notes the similarity of their elemental composition. Crucial for understanding chemical nature proteins had a release during their hydrolysis of amino acids. The first discovered amino acid was, apparently, asparagine, isolated by L. Vauquelin from the juice of Asparagus asparagus (1806). At the same time, J. Proust received leucine from the decomposition of cheese and cottage cheese. Then, many other amino acids were isolated from the products of protein hydrolysis.
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Proteins are complex organic matter that perform important functions in the cell. They are giant polymeric molecules whose monomers are amino acids. Each amino acid has a carboxyl group (-COOH) and an amino group (-NH2). The presence of acidic and basic groups in one molecule determines their high reactivity. Between the connected amino acids, a chemical bond arises, called a peptide, and the resulting compound of several amino acids is called a peptide. More than 150 different amino acids are known in nature, but only 20 are usually involved in the construction of proteins of living organisms. Valine, leucine, isoleucine, phenylalanine, methionine, tryptophan, threonine, lysine are indispensable for humans.
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The primary structure of a protein is due to peptide bonds. The secondary one is a helix with hydrogen bonds. The tertiary one is tighter, the helix with sulfide bonds is a globule. Proteins begin to perform their functions. Quaternary - combines several globules (hemoglobin).
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Functions of proteins. Building - proteins are an integral part of all parts of the body. Enzymatic - proteins accelerate the course of all chemical reactions necessary for the life of the organism. Motor - proteins provide contraction of muscle fibers, movement of cilia and flagella, movement of chromosomes during cell division, movement of plant organs. Transport - proteins carry various substances inside the body. Energy - protein breakdown serves as a source of energy for organisms. Protective - proteins recognize and destroy substances dangerous to the body, etc. Signal - a reaction to changes in physical, chemical factors. Regulatory - hormone proteins affect metabolism.
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Purpose: to prove the catalytic action of proteins - enzymes, to show their high specificity, as well as the highest activity in a physiological environment. Equipment: Petri dish, starched tissue, sucrose solution, 1% iodine solution in potassium iodide, cotton swab. Conclusion: Saliva amylase breaks down starch for glucose, glucose does not give a blue color with iodine, so we observe a pattern of white stripes on the fabric.
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Purpose: to prove the presence in biological objects of such important organic substances as proteins. Equipment: Test tube, egg white, gauze, distilled water, sodium hydroxide, copper sulfate, Nitric acid.CuSO4 + 2NaOH = Cu(OH)2 + Na2SO4 Cu(OH)2 + albumin - violet color Conclusion: The appearance of a violet color is proof of the protein in solution.
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Proteins are an essential component of all living cells, they play an important role in wildlife, they are the main, valuable and indispensable component of nutrition, the basis structural elements and tissues, support the metabolism and energy, participate in the processes of growth and reproduction, provide the mechanisms of movement, the development of immune responses, are necessary for the functioning of all organs and systems of the body. Knowledge of the process of protein biosynthesis in a living cell is of great importance for practical solution tasks in the area Agriculture, industry, medicine, environmental protection. Their solution is impossible without knowledge of the laws of genetics. The latest achievements in genetics are associated with the development of genetic engineering. Genetic engineering has made it possible to produce relatively cheaply in large quantities almost any protein.
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Belyaev D.K., Ruvinsky A.O. "General biology", M., "Enlightenment", 1991 Berezin B.D., Berezin D.B. Course of modern organic chemistry. Tutorial for universities. -M., " graduate School”, 1999. Brem Z., Meinke I. “Biology. Handbook of schoolchildren and students”, M., “Drofa”, 1999. Zayats R.G., Rachkovskaya I.V., Stambrovskaya V.M. "Biology manual for applicants", Minsk, "Higher School", 1996. Zubritskaya A.V. "Molecular Biology" Grade 10, "Corypheus"; Volgograd, 2006. Polyansky Yu.I. "General biology", M., "Enlightenment", 2000 Ponomareva I.N., Kornilova O.A., Chernova N.M. "Fundamentals general biology”, M., “Ventana-Graf”, 2005. Taylor D., Green N., Stout W., “Biology” Volume 1 Publishing house “Mir”, Moscow, 2008. Tritak D.I. "Biology. Reference materials”, M., “Enlightenment”, 1994. Chemistry-reference book for applicants and students. M., "AST-Folio", 2000. Encyclopedia for children Chemistry, M., "Avanta +", 2000. Encyclopedia for children Biology, M., "Avanta +", 1998.
Content. Introduction I. History of protein discovery II. The structure of proteins. 1. The structure of proteins; 2. Spatial structure; 3. Properties of proteins; III. Functions of proteins. IV.Practical work. 1.Protein denaturation; 2. Proof of the functioning of proteins as biocatalysts 3. Color reactions for proteins V. Conclusion. VI. Literature.
Introduction. F. Engels Proteins are natural organic compounds that provide all the life processes of any organism. "Life is a way of existence of protein bodies." Based on the achievements of contemporary natural science, F. Engels laid the scientific philosophical and theoretical foundations of ideas about life and protein as its most essential carrier and determinant. The correctness of the theory of F. Engels is fully confirmed by modern biological chemistry, molecular biology and biophysics, which have more versatile experimental data, both on the chemical structure of proteins, and on their role and significance in life.
Discovery history. Squirrels got their name from egg white, which has been used by man since time immemorial as an integral part of food. According to the descriptions of Pliny the Elder, already in ancient Rome, egg white was also used as a remedy. However, the true history of protein substances begins when the first information about the properties of proteins as chemical compounds appears (clotting when heated, decomposition by acids and strong alkalis, etc.).
By the beginning of the 19th century, the first works on the chemical study of proteins appeared. Already in 1803, J. Dalton gives the first formulas of proteins - albumin and gelatin - as substances containing nitrogen. In 1810, J. Gay-Lussac conducts chemical analyzes of proteins - blood fibrin, casein and notes the similarity of their elemental composition. Of decisive importance for understanding the chemical nature of proteins was the isolation of amino acids during their hydrolysis. The first discovered amino acid was, apparently, asparagine, isolated by L. Vauquelin from the juice of Asparagus asparagus (1806). At the same time, J. Proust received leucine from the decomposition of cheese and cottage cheese. Then, many other amino acids were isolated from the products of protein hydrolysis.
Discovery of amino acids in proteins. Amino acidyearsourceWho first isolated Glycine1820gelatinA. Braconno Tyrosine1848CaseinF.Bopp Serine1865SilkE. Kramer Glutamic acid 1866 Plant proteins G. Ritthausen Lysine 1895 CaseinE. Drexel Cystine 1899 Horn substance K. Merner Tryptophan 1902 Casein F. Hopkins, D.Col Isoleucine1904fibrinF. Erlich Threonine 1925 Oat Proteins S. Shriver
The structure of proteins. Proteins are complex organic substances that perform important functions in the cell. They are giant polymeric molecules whose monomers are amino acids. Each amino acid has a carboxyl group (-COOH) and an amino group (-NH 2). The presence of acidic and basic groups in one molecule determines their high reactivity. Between the connected amino acids, a chemical bond arises, called a peptide, and the resulting compound of several amino acids is called a peptide. More than 150 different amino acids are known in nature, but only 20 are usually involved in the construction of proteins of living organisms. Valine, leucine, isoleucine, phenylalanine, methionine, tryptophan, threonine, lysine are indispensable for humans.
The secondary is a helix with hydrogen bonds. The primary structure of a protein is due to peptide bonds. Tertiary - tighter, helix with sulfide bonds - a globule. Proteins begin to perform their functions. Quaternary - combines several globules (hemoglobin).
Denaturation depends: 1) on the time of exposure 2) on the nature of the protein 3) on the strength of the acting factor Influencing factors: a) temperature increase b) radiation c) alkali and acids d) heavy metals e) alcohol e) pressure Properties of proteins. Denaturation is the destruction of the structure of a protein. Renaturation is the process of restoring the structure of a protein.
Protein functions. 1. Building - proteins are an integral part of all parts of the body. 2. Enzymatic - proteins accelerate the course of all chemical reactions necessary for the life of the body. 3. Motor - proteins provide contraction of muscle fibers, movement of cilia and flagella, movement of chromosomes during cell division, movement of plant organs. 4. Transport - proteins carry various substances inside the body. 5. Energy - protein breakdown serves as a source of energy for organisms. 6. Protective - proteins recognize and destroy substances dangerous to the body, etc. 7. Signal - a reaction to changes in physical, chemical factors. 8. Regulatory - hormone proteins affect metabolism.
Practical work. 1. Denaturation of proteins with alcohol. Purpose: to consider the process of protein denaturation. Equipment: Protein solution, test tube, alcohol. I. I pour 1 ml of chicken egg protein solution into a test tube. II. Add a few drops of ethyl alcohol. Conclusion: when the protein interacts with alcohol, we observe the precipitation of an insoluble precipitate, which means that the protein is denatured.
2. Evidence for the functioning of proteins as biocatalysts. Purpose: to prove the catalytic action of proteins - enzymes, to show their high specificity, as well as the highest activity in a physiological environment. Equipment: Petri dish, starched cloth, sucrose solution, 1% solution of iodine in potassium iodide, cotton swab. Conclusion: Salivary amylase breaks down starch into glucose, glucose does not give a blue color with iodine, therefore we observe a pattern of white stripes on the fabric.
3. Detection of proteins in biological objects. Qualitative reactions to proteins (biuret). Purpose: to prove the presence in biological objects of such important organic substances as proteins. Equipment: Test tube, egg white, gauze, distilled water, sodium hydroxide, copper sulfate, nitric acid. CuSO 4 + 2NaOH = Cu(OH) 2 + Na 2 SO 4 Cu(OH) 2 + albumin - violet color Conclusion: The appearance of a violet color is proof of the protein in solution.
Proteins are an obligatory component of all living cells, they play an important role in wildlife, they are the main, valuable and irreplaceable component of nutrition, the basis of structural elements and tissues, support metabolism and energy, participate in the processes of growth and reproduction, provide mechanisms for movements, the development of immune responses, necessary for the functioning of all organs and systems of the body. Knowledge of the process of protein biosynthesis in a living cell is of great importance for the practical solution of problems in the field of agriculture, industry, medicine, and nature conservation. Their solution is impossible without knowledge of the laws of genetics. The latest achievements in genetics are associated with the development of genetic engineering. Genetic engineering has made it possible to produce relatively cheaply in large quantities almost any protein. Conclusion.
Literature. 1. Belyaev D.K., Ruvinsky A.O. "General biology", M., "Enlightenment", 1991. 2. Berezin B.D., Berezin D.B. Course of modern organic chemistry. Textbook for universities. M., "Higher School", 1999. 3. Brem Z., Meinke I. “Biology. Reference book for schoolchildren and students”, M., “Drofa”, 1999. 4. Zayats R.G., Rachkovskaya I.V., Stambrovskaya V.M. "Biology manual for applicants", Minsk, "Higher School", 1996. 5.Zubritskaya A.V. "Molecular Biology" Grade 10, "Corypheus"; Volgograd, 2006 6. Polyansky Yu.I. "General biology", M., "Enlightenment", 2000. 7. Ponomareva I.N., Kornilova O.A., Chernova N.M. "Fundamentals of General Biology", M., "Ventana-Graf", 2005. 8. Taylor D., Green N., Stout W., "Biology" Volume 1 Publishing house "Mir", Moscow, 2008. 9. Traitak D.I. "Biology. Reference materials”, M., “Enlightenment”, 1994. 10. Chemistry reference book for applicants and students. M., "AST-Folio", 2000. 11. Encyclopedia for children Chemistry, M., "Avanta +", 2000. 12. Encyclopedia for children Biology, M., "Avanta +", 1998
What proteins are called acidic? Proteins with more acidic amino acids that lower the pH. What proteins are called neutral? Proteins in which the same number of carboxyl and amino groups. Why are proteins powerful buffer systems? Able to attach or give hydrogen ions, maintaining a certain pH level. What is protein denaturation? The process of losing the three-dimensional conformation inherent in a given protein molecule is called denaturation. What is renaturation? The process of restoring the protein structure after denaturation is called renaturation. Give examples of soluble and insoluble proteins: Soluble (blood plasma proteins - fibrinogen, prothrombin, albumin, globulins), insoluble proteins that perform mechanical functions (fibroin, keratin, collagen). Give examples of proteins that are resistant to external influences: Fibroin is a web protein, keratin is a hair protein, collagen is a tendon protein.
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The presentation on the topic "Protein Functions" can be downloaded absolutely free of charge on our website. Project subject: Biology. Colorful slides and illustrations will help you keep your classmates or audience interested. To view the content, use the player, or if you want to download the report, click on the appropriate text under the player. The presentation contains 19 slide(s).
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Proteins (proteins, polypeptides) are high-molecular organic substances consisting of alpha-amino acids connected in a chain by a peptide bond. Proteins are an important part of the nutrition of animals and humans, since all the necessary amino acids cannot be synthesized in their bodies and some of them come with protein foods. During digestion, enzymes break down ingested proteins into amino acids, which are used in the body's protein biosynthesis or further broken down for energy.
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Functions of proteins
The functions of proteins in the cells of living organisms are more diverse than the functions of other biopolymers - polysaccharides and DNA. Thus, enzyme proteins catalyze the course of biochemical reactions and play an important role in metabolism. Eukaryotic cytoskeleton (Fig. 1) Some proteins perform a structural or mechanical function, forming a cytoskeleton (Fig. 1) that maintains the shape of cells. Proteins also play an important role in cell signaling systems, in the immune response and in the cell cycle.
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structural function.
The structural function of proteins is that proteins are involved in the formation of almost all cell organelles, largely determining their structure (shape); form a cytoskeleton that gives shape to cells and many organelles and provides the mechanical shape of a number of tissues; are part of the intercellular substance, which largely determines the structure of tissues and the shape of the body of animals. Structural proteins include: - collagen - actin - elastin - myosin - keratin - tubulin
protein keratin
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catalytic function. (enzymatic)
The most well-known role of proteins in the body is the catalysis of various chemical reactions. Enzymes are a group of proteins with specific catalytic properties, that is, each enzyme catalyzes one or more similar reactions, accelerating them. Example: 2H202 → 2H20 + 02 In the presence of iron salts (catalyst), this reaction is somewhat faster. Catalase enzyme for 1 sec. splits up to 100 thousand H202 molecules. Molecules that attach to an enzyme and change as a result of the reaction are called substrates. The mass of the enzyme is much greater than the mass of the substrate. The part of the enzyme that attaches the substrates contains catalytic amino acids, called the active site of the enzyme.
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motor function.
Muscle contraction is a process during which the chemical energy stored in the form of high-energy pyrophosphate bonds in ATP molecules is converted into mechanical work. Direct participants in the contraction process are two proteins - actin and myosin. Special contractile proteins (actin and myosin) are involved in all types of cell and organism movement: the formation of pseudopodia, the flickering of cilia and the beating of flagella in protozoa, muscle contraction in multicellular animals, the movement of leaves in plants, etc.
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transport function.
The transport function of proteins is the participation of proteins in the transfer of substances into and out of cells, in their movements inside cells, as well as in their transport by blood and other fluids throughout the body. There are different types of transport that are carried out with the help of proteins.
Transport of substances across the cell membrane
Transport of substances within the cell
Transport of substances throughout the body
For example, hemoglob and blood carries oxygen
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protective function.
Protect the body from invading foreign organisms and from damage
Antibodies block foreign proteins
For example, fibrinogen and prothrombin provide blood clotting
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Energy function.
Energy function - proteins serve as one of the sources of energy in the cell. The breakdown of 1 g of protein to final products releases 17.6 kJ of energy. First, proteins break down to amino acids, and then to final products: -water, -carbon dioxide, -ammonia. But proteins are rarely used as an energy source.
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receptor function.
Receptor proteins are protein molecules embedded in the membrane that can change their structure in response to the addition of a specific chemical substance.
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immune function. (antibiotics)
At the moment when pathogens - viruses or bacteria - enter the body, special proteins begin to be produced in specialized organs - antibodies that bind and neutralize pathogens. The peculiarity of the immune system is that, due to antibodies, it can fight almost any kind of pathogens. Interferons are also protective proteins of the immune system. These proteins are produced by cells infected with viruses. Their effect on neighboring cells provides antiviral resistance by blocking the reproduction of viruses or the assembly of viral particles in target cells. Interferons also have other mechanisms of action, for example, they affect the activity of lymphocytes and other cells of the immune system.
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Toxins, toxic substances of natural origin. Usually, high-molecular compounds (proteins, polypeptides, etc.) are classified as toxins, which, when they enter the body, produce antibodies. According to the target of action, toxins are divided into - Hematic poisons - poisons that affect the blood. -Neurotoxins - poisons that affect nervous system and brain. Myoxic poisons are poisons that damage muscles. -Hemotoxins are toxins that damage blood vessels and cause bleeding. Hemolytic toxins are toxins that damage red blood cells. -Nephrotoxins are toxins that damage the kidneys. - Cardiotoxins are toxins that damage the heart. - Necrotoxins - toxins that destroy tissues, causing their necrosis (necrosis). Consider plant poisons: Fallotoxins and amatoxins are found in various species: pale grebe, smelly fly agaric, spring. White toadstool (Fig. 1) - a deadly poisonous mushroom, contains the poisons of amanitin and virozin. For humans, the lethal dose of a-amanitin is 5-7 mg, phalloidin 20-30 mg (on average, one mushroom contains up to 10 mg of phalloidin, 8 mg of L-amanitin and 5 mg of B-amanitin). When poisoned, death occurs.
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contraction function.
Proteins are involved in the contraction of muscle fibers. contraction function. Many protein substances are involved in the act of muscle contraction and relaxation. However leading role in these vital important processes play actin and myosin - specific proteins of muscle tissue. The contractile function is inherent not only in muscle proteins, but also in cytoskeletal proteins, which ensures the finest processes of cell vital activity (chromosome segregation during mitosis).
Actin and myosin are muscle proteins
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hormonal function.
hormonal function. Metabolism in the body is regulated by various mechanisms. In this regulation, an important place is occupied by hormones synthesized not only in the endocrine glands, but also in many other cells of the body (see below). A number of hormones are represented by proteins or polypeptides, such as hormones of the pituitary gland, pancreas, etc. Some hormones are derivatives of amino acids.
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nutritional function. (backup)
Nutritional (reserve) function. This function is performed by the so-called reserve proteins, which are sources of nutrition for the fetus, such as egg proteins (ovalbumins). The main protein of milk (casein) also performs a mainly nutritional function. A number of other proteins are used in the body as a source of amino acids, which in turn are precursors of biologically active substances that regulate metabolic processes. Milk casein Egg albumin
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regulatory function.
Some proteins are hormones. Hormones - biologically active substances, released into the blood by various glands that are involved in the regulation of metabolic processes. The hormone insulin regulates the level of carbohydrates in the blood.
"Proteins and their functions" - 1 g of protein is equivalent to 17.6 kJ. The concept of proteins. Transport function of proteins. Construction material. Energy function. Transformation of proteins in the body. Chemical properties proteins. protective function. Secondary structure Tertiary structure Quaternary structure.
"Proteins substance" - Dietary proteins. Quaternary. Make up the cytoskeleton of the cell. Quaternary structure. They have only a few proteins. The coil is held due to the bonds that arise between the AA radicals. Consist of a large number of AK. energy proteins. Insoluble proteins are fibrillar. Used by the body for movement.
"Protein Biosynthesis Biology" - W. The main function of ribosomes is the synthesis of proteins. Such a complex is called a polysome. I know and can: Translation is the translation of a nucleotide sequence into a protein amino acid sequence. D. Ribosomes are very small cell organelles formed ribonucleic acids and proteins. "We are all heirs of DNA."
"Protein biosynthesis" - 7. Contents. Biosynthesis of proteins in a living cell. 9. 6. 3. References. 10. 5. Scheme of plant and animal cells. Participants in the biosynthesis of protein molecules. Introduction. 12.
"Biosynthesis of proteins" - Test yourself. The value of proteins. Translation (lat. transfer, translation). Synthesis of a polypeptide chain on a ribosome. 6. A segment of DNA is given: C-G-A-T-T-A-G-C-G-G-A-A-C-A-C. Transcription Broadcast. Content. Energy of biosynthesis. Lesson topic: Protein biosynthesis.
“Protein Functions” - 6. The signaling function of proteins is very important for cell life. The motor function is performed by: special contractile proteins in flagella, cilia, muscles. Able to attach or give hydrogen ions, maintaining a certain pH level. One of the most important functions of proteins. For example, insulin regulates blood sugar levels.
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