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Organic and Inorganic Compounds Presented by: Mrs. Knopke FUHS Science Dept.

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Presentation on theme: "Organic and Inorganic Compounds Presented by: Mrs. Knopke FUHS Science Dept."— Presentation transcript:

1 Organic and Inorganic Compounds Presented by: Mrs. Knopke FUHS Science Dept.

2 Elements found in Living Systems The three commonest chemical elements of life are : Carbon Hydrogen Oxygen They are part of all the main organic compounds in living organism

3 Examples of Chemical Elements and Their Roles Element Role in plants and animals NitrogenPart of the amine groups of amino acids and therefore proteins. CalciumNeeded to make the mineral that strengthens bones and teeth. PhosphorusPart of the phosphate groups in ATP and DNA molecules. IronNeeded to make Hemoglobin and thus to carry oxygen in blood. SodiumUsed in neurons ( nerve cells) for the transmission of nerve impulses.

4 Organic and inorganic compounds: Living organisms contain many chemical compounds. Some on them are organic and some inorganic: Organic: compounds containing carbon that are found in living organism. ex. Proteins, Carbohydrates, Lipids and Nucleic Acids

5 Inorganic compounds: There are a few carbon compounds that are inorganic even though they can be found in living organisms: These are single carbon compounds that are also widely found in the environment. Carbon Dioxides Carbonates and Hydrogen Carbonates

6 Subunits of Organic Compounds: The molecules of many organic compounds are large and may seem complex, but they are built up using small and relatively simple subunits: Important Subunits Protein Subunits: Amino Acids

7 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings One group of amino acids has hydrophobic R groups. Fig. 5.15a

8 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Another group of amino acids has polar R groups, making them hydrophilic. Fig. 5.15b

9 The last group of amino acids includes those with functional groups that are charged (ionized) at cellular pH. Some R groups are bases, others are acids. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.15c

10 Proteins are instrumental in about everything that an organism does. These functions include structural support, storage, transport of other substances, intercellular signaling, movement, and defense against foreign substances. Proteins are the overwhelming enzymes in a cell and regulate metabolism by selectively accelerating chemical reactions. Humans have tens of thousands of different proteins, each with their own structure and function.

11 Function of Proteins: A protein’s specific conformation determines its function. In almost every case, the function depends on its ability to recognize and bind to some other molecule. For example, antibodies bind to particular foreign substances that fit their binding sites. Enzyme recognize and bind to specific substrates, facilitating a chemical reaction. Neurotransmitters pass signals from one cell to another by binding to receptor sites on proteins in the membrane of the receiving cell.

12 Proteins have four main structures:

13 The primary structure of a protein is its unique sequence of amino acids. Lysozyme, an enzyme that attacks bacteria, consists on a polypeptide chain of 129 amino acids. The precise primary structure of a protein is determined by inherited genetic information. Fig. 5.18

14 Even a slight change in primary structure can affect a protein’s conformation and ability to function. In individuals with sickle cell disease, abnormal hemoglobins, oxygen-carrying proteins, develop because of a single amino acid substitution. These abnormal hemoglobins crystallize, deforming the red blood cells and leading to clogs in tiny blood vessels. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

15 Fig Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

16 The secondary structure of a protein results from hydrogen bonds at regular intervals along the polypeptide backbone. Typical shapes that develop from secondary structure are coils (an alpha helix) or folds (beta pleated sheets). Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.20

17 The structural properties of silk are due to beta pleated sheets. The presence of so many hydrogen bonds makes each silk fiber stronger than steel. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.21

18 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Tertiary structure is determined by a variety of interactions among R groups and between R groups and the polypeptide backbone. These interactions include hydrogen bonds among polar and/or charged areas, ionic bonds between charged R groups, and hydrophobic interactions and van der Waals interactions among hydrophobic R groups. Fig. 5.22

19 While these three interactions are relatively weak, disulfide bridges, strong covalent bonds that form between the sulfhydryl groups (SH) of cysteine monomers, stabilize the structure. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.22

20 Quarternary structure results from the aggregation of two or more polypeptide subunits. Collagen is a fibrous protein of three polypeptides that are supercoiled like a rope. This provides the structural strength for their role in connective tissue. Hemoglobin is a globular protein with two copies of two kinds of polypeptides. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.23

21 A protein’s conformation can change in response to the physical and chemical conditions. Alterations in pH, salt concentration, temperature, or other factors can unravel or denature a protein. These forces disrupt the hydrogen bonds, ionic bonds, and disulfide bridges that maintain the protein’s shape. Some proteins can return to their functional shape after denaturation, but others cannot, especially in the crowded environment of the cell. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

22 Fig. 5.25

23 Carbohydrate subunits Glucose

24 Examples of Carbohydrates Monosaccharides Glucose, fructose, and ribose Disaccharides Sucrose (glucose + fructose) Polysaccharides Starch (made of glucose subunits) Glycogen (made of glucose subunits, but linked differently from starch)

25 Functions of Carbohydrates: Transport – glucose is carried by the blood to transport energy to cells throughout the body. Energy Storage – Energy is stored in the form of glycogen in liver cells

26 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.3

27 Monosaccharides, particularly glucose, are a major fuel for cellular work. They also function as the raw material for the synthesis of other monomers, including those of amino acids and fatty acids. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.4

28 Two monosaccharides can join with a glycosidic linkage to form a dissaccharide via dehydration. Maltose, malt sugar, is formed by joining two glucose molecules. Sucrose, table sugar, is formed by joining glucose and fructose and is the major transport form of sugars in plants. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.5a

29 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.5 While often drawn as a linear skeleton, in aqueous solutions monosaccharides form rings.

30 Polysaccharides are polymers of hundreds to thousands of monosaccharides joined by glycosidic linkages. One function of polysaccharides is as an energy storage macromolecule that is hydrolyzed as needed. Other polysaccharides serve as building materials for the cell or whole organism. 2. Polysaccharides, the polymers of sugars, have storage and structural roles Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

31 Starch is a storage polysaccharide composed entirely of glucose monomers. Most monomers are joined by 1-4 linkages between the glucose molecules. One unbranched form of starch, amylose, forms a helix. Branched forms, like amylopectin, are more complex. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.6a

32 Plants store starch within plastids, including chloroplasts. Plants can store surplus glucose in starch and withdraw it when needed for energy or carbon. Animals that feed on plants, especially parts rich in starch, can also access this starch to support their own metabolism. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

33 Animals also store glucose in a polysaccharide called glycogen. Glycogen is highly branched, like amylopectin. Humans and other vertebrates store glycogen in the liver and muscles but only have about a one day supply. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Insert Fig. 5.6b - glycogen Fig. 5.6b

34 While polysaccharides can be built from a variety of monosaccharides, glucose is the primary monomer used in polysaccharides. One key difference among polysaccharides develops from 2 possible ring structure of glucose. These two ring forms differ in whether the hydroxyl group attached to the number 1 carbon is fixed above (beta glucose) or below (alpha glucose) the ring plane. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.7a

35 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.7 Starch is a polysaccharide of alpha glucose monomers.

36 Structural polysaccharides form strong building materials. Cellulose is a major component of the tough wall of plant cells. Cellulose is also a polymer of glucose monomers, but using beta rings. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.7c

37 While polymers built with alpha glucose form helical structures, polymers built with beta glucose form straight structures. This allows H atoms on one strand to form hydrogen bonds with OH groups on other strands. Groups of polymers form strong strands, microfibrils, that are basic building material for plants (and humans). Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

38 Fig. 5.8

39 The enzymes that digest starch cannot hydrolyze the beta linkages in cellulose. Cellulose in our food passes through the digestive tract and is eliminated in feces as “insoluble fiber”. As it travels through the digestive tract, it abrades the intestinal walls and stimulates the secretion of mucus. Some microbes can digest cellulose to its glucose monomers through the use of cellulase enzymes. Many eukaryotic herbivores, like cows and termites, have symbiotic relationships with cellulolytic microbes, allowing them access to this rich source of energy. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

40 Another important structural polysaccharide is chitin, used in the exoskeletons of arthropods (including insects, spiders, and crustaceans). Chitin is similar to cellulose, except that it contains a nitrogen-containing appendage on each glucose. Pure chitin is leathery, but the addition of calcium carbonate hardens the chitin. Chitin also forms the structural support for the cell walls of many fungi. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.9

41 Lipid Subunits: 2 parts Fatty Acids Glycerol

42 Function of Lipids: Energy storage – in the form of fat in humans and oil in plants. Heat Insulation – a layer of fat under the skin reduces heat loss. Bouyancy – Lipids are less dense than water so help animals to float.

43 saturated fatty acid - a hydrogen at every possible position.

44 unsaturated fatty acid - formed by the removal of hydrogen atoms from the carbon skeleton.

45 Phospholipids have two fatty acids attached to glycerol and a phosphate group at the third position. The phosphate group carries a negative charge. Additional smaller groups may be attached to the phosphate group. 2. Phospholipids are major components of cell membranes Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

46 Fig The interaction of phospholipids with water is complex. The fatty acid tails are hydrophobic, but the phosphate group and its attachments form a hydrophilic head.

47 When phospholipids are added to water, they self-assemble into aggregates with the hydrophobic tails pointing toward the center and the hydrophilic heads on the outside. This type of structure is called a micelle. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.13a

48 At the surface of a cell phospholipids are arranged as a bilayer. Again, the hydrophilic heads are on the outside in contact with the aqueous solution and the hydrophobic tails from the core. The phospholipid bilayer forms a barrier between the cell and the external environment. They are the major component of membranes. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.12b

49 Steroids are lipids with a carbon skeleton consisting of four fused carbon rings. Different steroids are created by varying functional groups attached to the rings. 3. Steroids include cholesterol and certain hormones Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.14

50 Cholesterol, an important steroid, is a component in animal cell membranes. Cholesterol is also the precursor from which all other steroids are synthesized. Many of these other steroids are hormones, including the vertebrate sex hormones. While cholesterol is clearly an essential molecule, high levels of cholesterol in the blood may contribute to cardiovascular disease. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

51 Carbohydrates and Lipids in Energy Storage Advantages ofAdvantages of LipidsCarbo’s 1. More energy per gram, 1. Carbohydrates are more stores of lipids are easily digested than lipids lighter then stores of so the energy stored by Carbo’s that contain the them can be released more Same amount of energy. Rapidly. 2. Lipids are insoluble in 2. Carbohydrates are soluble water, so they do not in water so are easier to cause problems with transport to and from Osmosis in cells storage. 3. Energy storage for 3. Energy storage for short Long-term periods.

52 Nucleotide subunits: 3 parts These make up the rungs of the ladder Pyrimidines C, T and U Purines A and G These make up the backbone of DNA Deoxyribose or Ribose Phosphate Group

53 There are two types of nucleic acids: ribonucleic acid (RNA) and deoxyribonucleic acid (DNA). DNA provides direction for its own replication. DNA also directs RNA synthesis and, through RNA, controls protein synthesis.

54 The sugar-phosphate backbones of the two polynucleotides are on the outside of the helix. Pairs of nitrogenous bases, one from each strand, connect the polynucleotide chains with hydrogen bonds. Most DNA molecules have thousands to millions of base pairs. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Fig. 5.30

55

56 Genes code for proteins: The amino acid sequence of a polypeptide is programmed by a gene. A gene consists of regions of DNA, a polymer of nucleic acids. DNA (and their genes) is passed by the mechanisms of inheritance.

57 How Larger Molecules are made: Condensation Reactions In a condensation reaction two molecules are joined together to form a larger molecule. Water is also formed in the reaction.

58 Creating a Dipeptide: Condensation of two Amino Acids to form a dipeptides and water + H 2 O

59 Further condensations forming a Polypeptide

60 Condensation can be used to build Carbohydrates Disaccharide Polysaccharides

61 and Lipids forming Triglycerides

62 Hydrolysis Reactions: Large molecules such as polypeptides, polysaccharides and triglycerides can be broken down into smaller molecules by hydrolysis reactions. Water molecules are used up. Reverse of Condensation Polypeptides + Water Dipeptides or Amino Acids Polysaccharides + Water Disaccharides and Monosaccharides Glycerides + Water Fatty Acids + Glycerol


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