Presentation on the topic "Organic substances in the cell" in biology in powerpoint format. This presentation for 9th grade schoolchildren tells about the structural features and functions of proteins, nucleic acids - organic substances that form the basis of all life on Earth. The work contains a large number of questions and tasks on the topic. Presentation author: Ekaterina Viktorovna Korotkova, teacher of biology and chemistry.

Fragments from the presentation

Biological dictation

1. All organic substances are highly soluble in water
2. Fats are a source of energy and water
3. Chemical elements in a cell are completely different from those in inanimate nature
4. Iron accumulates in apples, and iodine accumulates in seaweed
5. The same elements are part of living and inanimate nature, which indicates their unity
6. The most common inorganic substance is water.
7. The more actively an organ works, the less water there is in its cells.
8. Hemoglobin is the red protein in our blood.
9. To be healthy, a person should receive 100 g of protein per day from food.
10. Carbohydrates are needed only by plants
11. The cell contains organic and inorganic substances

Task 1:

The patient has low hemoglobin. Iron deficiency anemia, anemia. What medicines and fruits can you offer to help him?

Task 2:

The patient is very nervous and irritable. He probably has a thyroid disease - goiter. What can you offer?

Task 3:

The criminal, in order to hide traces of the crime, burned the victim's bloody clothes. However, a forensic examination based on ash analysis established the presence of blood on the clothing. How?

Squirrels

• Bulk cell mass 50-70%
• Squirrels- These are complex organic substances, which are polymer molecules whose monomers are amino acids.

Functions of proteins

• Enzymatic;
• Transport;
• Structural;
• Protective...

Nucleic acids

• Deoxyribonucleic acid - DNA
• Ribonucleic acid - RNA
• Nucleic acid molecules are very long polymer chains (strands), the monomers of which are nucleotides

Nucleotide structure

Nucleotide structure. Nitrogenous bases

• Adenine
• Guanine
• Cytosine
• Timin

• Adenine
• Guanine
• Cytosine
• Uracil

DNA

• Consists of two polynucleotide chains
• G---C
• Principle of complementarity

Exercise 1:

• Compose a chain of a DNA molecule according to the principle of complementarity, indicate the connections between nitrogenous bases:
• -T-G-C-T-A-G-C-T-A-G-C-A-A-T-T-

RNA as opposed to DNA

• Consists of one chain
• Instead of deoxyribose - ribose
• Instead of Timin - Uracil

Task 2:

• Independent work with the textbook § 6:
• Find the functions of an RNA molecule
• Types of RNA by function

Squirrels (proteins, polypeptides) are the most numerous, most diverse and of paramount importance biopolymers. Protein molecules contain atoms of carbon, oxygen, hydrogen, nitrogen and sometimes sulfur, phosphorus and iron.

Protein monomers are amino acids, which (having carboxyl and amino groups) have the properties of an acid and a base (amphoternic).

Thanks to this, amino acids can connect with each other (their number in one molecule can reach several hundred). In this regard, protein molecules are large in size and are called macromolecules.

Structure of a protein molecule

Under structure of a protein molecule understand its amino acid composition, the sequence of monomers and the degree of twisting of the protein molecule.

There are only 20 types of different amino acids in protein molecules, and a huge variety of proteins is created due to their different combinations.

• The sequence of amino acids in a polypeptide chain is protein primary structure(it is unique to any protein and determines its shape, properties and functions). The primary structure of a protein is unique to any type of protein and determines the shape of its molecule, its properties and functions.
• A long protein molecule folds and first takes on the appearance of a spiral as a result of the formation of hydrogen bonds between the -CO and -NH groups of different amino acid residues of the polypeptide chain (between the carbon of the carboxyl group of one amino acid and the nitrogen of the amino group of another amino acid). This spiral is protein secondary structure.
• Protein tertiary structure- three-dimensional spatial “packaging” of the polypeptide chain in the form globules(ball). The strength of the tertiary structure is ensured by a variety of bonds that arise between amino acid radicals (hydrophobic, hydrogen, ionic and disulfide S-S bonds).
• Some proteins (for example, human hemoglobin) have quaternary structure. It arises as a result of the combination of several macromolecules with a tertiary structure into a complex complex. The quaternary structure is held together by weak ionic, hydrogen and hydrophobic bonds.

The structure of proteins can be disrupted (subjected to denaturation) when heated, treated with certain chemicals, irradiated, etc. With weak exposure, only the quaternary structure disintegrates, with stronger exposure, the tertiary, and then the secondary, and the protein remains in the form of a polypeptide chain. As a result of denaturation, the protein loses its ability to perform its function.

Disruption of quaternary, tertiary and secondary structures is reversible. This process is called renaturation.

The destruction of the primary structure is irreversible.

In addition to simple proteins consisting only of amino acids, there are also complex proteins, which may include carbohydrates ( glycoproteins), fats ( lipoproteins), nucleic acids ( nucleoproteins) and etc.

Functions of proteins

• Catalytic (enzymatic) function. Special proteins - enzymes- capable of accelerating biochemical reactions in cells tens and hundreds of millions of times. Each enzyme speeds up one and only one reaction. Enzymes contain vitamins.

• Structural (construction) function- one of the main functions of proteins (proteins are part of cell membranes; keratin protein forms hair and nails; collagen and elastin proteins form cartilage and tendons).

• Transport function- proteins provide active transport of ions through cell membranes (transport proteins in the outer membrane of cells), transport of oxygen and carbon dioxide (blood hemoglobin and myoglobin in muscles), transport of fatty acids (blood serum proteins contribute to the transfer of lipids and fatty acids, various biologically active substances ).

• Signal function. Reception of signals from the external environment and transmission of information into the cell occurs due to proteins built into the membrane that are capable of changing their tertiary structure in response to the action of environmental factors.
• Contractile (motor) function- provided by contractile proteins - actin and myosin (thanks to contractile proteins, cilia and flagella move in protozoa, chromosomes move during cell division, muscles contract in multicellular organisms, and other types of movement in living organisms are improved).

• Protective function- antibodies provide immune protection of the body; fibrinogen and fibrin protect the body from blood loss by forming a blood clot.

• Regulatory function inherent in proteins - hormones(not all hormones are proteins!). They maintain constant concentrations of substances in the blood and cells, participate in growth, reproduction and other vital processes (for example, insulin regulates blood sugar).
• Energy function- during prolonged fasting, proteins can be used as an additional source of energy after carbohydrates and fats have been consumed (with the complete breakdown of 1 g of protein into final products, 17.6 kJ of energy is released). Amino acids released when protein molecules are broken down are used to build new proteins.

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Slide captions:

included in the cell. Akhatova O.V.

Organic substances are compounds containing carbon. Single or double bonds arise between carbon atoms, on the basis of which carbon chains are formed: linear, branched, cyclic. Most organic substances are polymers and consist of repeating particles called monomers. Regular biopolymers are substances consisting of identical monomers; irregular - consisting of different monomers.

Proteins are irregular biopolymers; monomers - 20 essential amino acids.

The amino group has the properties of a base. The radical group is different for everyone. The carboxyl group has acidic properties.

A peptide bond occurs between the joined amino acids, on the basis of which a compound is formed - a polypeptide.

Primary – linear, in the form of a polypeptide chain. Secondary - due to hydrogen bonds: spiral - a, accordion-shaped - b. Tertiary – globular, due to hydrophobic interactions. Quaternary - a combination of several molecules with a tertiary structure.

Proteins Simple Complex

GLOBULAR PROTEINS: antibodies, hormones, enzymes FIBRILLAR: collagen, skin keratin, elastin

Functions of proteins. Structural - are part of various cell organelles. Transport - the attachment of chemical elements to proteins and their transfer to certain cells. Motor - contractile proteins are involved in all movements of cells and the body. Catalytic – accelerate or slow down biochemical reactions in cells and organisms.

Functions of proteins. Energy – when 1g of protein is broken down, 17.6 kJ is released. Hormonal, or receptor, are part of many hormones. They take part in the regulation of life processes. Protective – antibodies (the most important molecules of the immune system) are proteins.

Milk contains casein.

Carbohydrates are cyclic molecules consisting of carbon, oxygen, and hydrogen and polymers consisting of the same cycles.

Monosaccharides Consist of one cycle (glucose) Disaccharides Consist of two cycles (sucrose) Polysaccharides Consist of many cycles (starch) Carbohydrates

Maltose. Glucose.

Lactose. Sucrose.

Cellulose. Chitin.

Functions of carbohydrates. Energy - can be broken down into carbon dioxide and soda with the release of energy. Structural - the walls of plant cells consist of carbohydrates (cellulose).

Lipids are compounds of two or three fatty acid molecules and a complex alcohol molecule.

Functions of lipids. Energy - can decay with the release of large amounts of energy. Serve for long-term energy storage. Construction – all cell membranes consist of lipids. Protective – lipid deposits in the form of a fatty layer provide thermal insulation for the body. Hormonal - some lipids are part of the hormones of the sex glands and adrenal glands.

Which statements are true? 1. Proteins are biopolymers. 2. Protein monomers are amino acids. 3. Wax, vitamin D, vegetable and animal fats are classified as lipids. 4. Proteins are the main source of energy. 5. Carbohydrates are carriers of hereditary information.

Which statements are true? 6. Glucose, sucrose are types of carbohydrates. 7.Fats are highly soluble in water. 8.Carbohydrates perform only a supporting function. 9.Fats serve as a reserve source of energy. 10. Proteins have only a primary structure.

Homework: P.22 to p. 111.

You did a great job!

In organisms and their metabolic products, a large number of carbon-containing compounds were found, characteristic only of living cells and organisms, called organic substances. Organic substances of cells Cells contain many organic molecules that are not found in inanimate nature. These include, in particular, proteins, carbohydrates, fats, nucleic acids, ATP.

Carbon Forms strong covalent bonds by sharing four electrons. Capable of forming stable chains and rings that serve as skeletons of macromolecules. It can form multiple covalent bonds with other carbon atoms, as well as with nitrogen and oxygen. a unique variety of organic molecules provide carbon with its special properties

Polymers Macromolecules - Molecules that are multi-link chains, making up about 90% of the mass of a dehydrated cell, are synthesized from simpler molecules called MONOMERS POLYMERS REGULAR IRREGULAR Natural polymers built from identical monomers, most of them (...- A - A - A - A -.. .) Polymers in which there is no specific pattern in the sequence of monomers (...A - B - C - B - A - B-...).

PROTEINS Proteins (Greek Protos - first, main) from the organic substances of the cell are in first place in quantity and importance. (in the tobacco mosaic virus - about molecules) Proteins account for about half of the dry mass of the cell. PROTEINS have a huge molecular weight and range from several thousand to several million. For example, Mr (insulin) = 5700; Mr (egg ambulin) = 36000; Mr (hemoglobin) =

The most complex among organic compounds. They contain hundreds (sometimes hundreds of thousands) of amino acid residues. The potential diversity of proteins is very large - each protein has its own special sequence of amino acids, controlled genetically. PROTEINS Carbohydrates and fats can be converted into each other in the body. Proteins can also be converted into fats and carbohydrates. However, fats and carbohydrates are not converted directly into proteins. Proteins, in addition to carbon, hydrogen and oxygen atoms (as in fats and carbohydrates), include nitrogen atoms!, as well as the metals Fe, Zn, Cu

PROTEINS There are proteins consisting of 3-8 amino acids, and there are proteins consisting of amino acid residues. Different protein molecules may differ from each other: By the number of amino acid units in the protein molecule. According to the order of amino acid units in the chain. According to the composition of amino acids in a polypeptide. A3 – A17 – A5 – A5 – A13 – A4 –– A5 – … – A2

AMINO ACIDS Plants synthesize all the amino acids they need themselves. Animals are capable of producing only half of them; the rest must be obtained from food in ready-made form. ESSENTIAL AMINO ACIDS Amino acids that are not synthesized in the animal body and must come from the environment.

FORMATION OF POLYPEPTIDE The joining of amino acids occurs through common groups: the amino group of one amino acid combines with the carboxyl group of another with the elimination of a water molecule. A strong covalent bond -NH-CO2- is formed between amino acids, which is called a peptide bond.

SPATIAL STRUCTURE OF PROTEIN Each protein has its own special geometric shape, structure or configuration. The primary structure of insulin was discovered by F. Sanger in 1944–54; The primary structure of several hundred proteins is currently known.

DENATURATION In many cases it is reversible, but not always. There are proteins that, after denaturation, are not able to restore lost structures, i.e. cannot RENATURATE the process of destruction of higher protein structures when the polypeptide molecule is exposed to various environmental factors (for example, temperature).
PROTEIN PROFESSIONS Structure-forming functions. (collagen, histones) Transport functions. (hemoglobin, prealbumin, ion channels) Protective functions. (immunoglobulin) Regulatory functions (somatropin, insulin) Catalysis. (enzymes) Motor functions. (actin, myosin) Spare functions.

HOMEWORK Study §, p. 90–99 1. Remember what role proteins play in the human body: insulin, pepsin, hemoglobin, fibrinogen, myosin. What protein function is it associated with? 2. Why do you think “life is a way of existence of protein bodies...”? 3. Think about the expression: “All enzymes are proteins, but not all proteins are enzymes.”

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 animal and human nutrition (main sources: meat, poultry, fish, milk, nuts, legumes, grains; to a lesser extent: vegetables, fruits, berries and mushrooms), since their bodies cannot synthesize all the necessary amino acids and some of which comes with protein foods. During the digestion process, enzymes break down consumed proteins into amino acids, which are used in the biosynthesis of body proteins or undergo further breakdown to produce energy. PROTEINS

The functions of proteins in a cell are very diverse. The most important of them is construction. Proteins are involved in the formation of all cell membranes and cell organelles. An important feature of proteins is their catalytic function. All biological catalysts and enzymes are protein in nature. FUNCTIONS OF PROTEINS

Motor function Motor function is provided by special contractile proteins. These proteins are involved in all the movements that cells and organisms are capable of: the flickering of cilia and the beating of flagella in protozoa, muscle contraction in multicellular animals, the movement of leaves in plants, etc. Transport function The transport function of proteins is the participation of proteins in the transfer of substances into cells and from cells, in their movements within cells, as well as in their transport by blood and other fluids throughout the body. Protective function They protect the body from the invasion of foreign proteins and microorganisms from damage. Thus, antibodies produced by lymphocytes block foreign proteins; fibrin and thrombin protect the body from blood loss. FUNCTIONS

Carbohydrates are organic substances containing a carbonyl group and several hydroxyl groups. The name of the class of compounds comes from the words “carbon hydrates” and was first proposed by K. Schmidt in 1844. Carbohydrates are a very broad class of organic compounds, among them there are substances with very different properties. This allows carbohydrates to perform a variety of functions in living organisms. Compounds of this class make up about 80% of the dry mass of plants and 23% of the dry mass of animals. CARBOHYDRATES

Carbohydrates have several functions in cells. They are an excellent source of energy for a large number of different processes occurring in our cells. Some carbohydrates may also have a structural function. For example, the substance that makes plants grow large and gives wood its strength is a polymeric form of glucose known as cellulose. Other types of polymeric sugars make up the reserve forms of energy known as starch and glycogen. Starch is found in plant foods such as potatoes, and glycogen is found in animals. Carbohydrates are essential for transmitting signals from one cell to another. They also contribute to the formation of contacts between cells and with the substance surrounding them in the body. The body's ability to resist infection by microbes, as well as the elimination of foreign substances from the body, also depends on the properties of carbohydrates. FUNCTIONS OF CARBOHYDRATES

Energy Carbohydrates serve as the main source of energy for the body. In the body and cell, carbohydrates have the ability to accumulate in the form of starch in plants and glycogen in animals. Starch and glycogen are a storage form of carbohydrates and are consumed as energy needs arise. With proper nutrition, up to 10% of glycogen can accumulate in the liver, and under unfavorable conditions its content can decrease to 0.2% of the liver mass. FUNCTIONS

Lipids are a wide group of organic compounds, including fatty acids, as well as their derivatives, both radical and carboxyl group. The previously used definition of lipids as a group of organic compounds that are highly soluble in non-polar organic solvents and practically insoluble in water is too vague. Daily requirement of an adult for lipids grams LIPIDS
Nucleic acid is a high-molecular organic compound, a biopolymer formed by nucleotide residues. Nucleic acids DNA and RNA are present in the cells of all living organisms and perform the most important functions for the storage, transmission and implementation of hereditary information. NUCLEIC ACIDS

Deoxyribonucleic acid (DNA) is a macromolecule that ensures storage, transmission from generation to generation and implementation of the genetic program for the development and functioning of living organisms. The main role of DNA in cells is the long-term storage of information about the structure of RNA and proteins. Ribonucleic acid (RNA) is one of the three main macromolecules found in the cells of all living organisms. TYPES OF NUCLEIC ACIDS