What is a double bond?

2 electrons lost from a metal atom

one pair of electrons shared between 4 atoms

one pair of electron shared between 2 atoms

Which of the following is a property of ionic compounds?

they contain no charged particles.

Chapter 4 Chemical Bonds

CARBOHYDRATES Carbohydrates are organic compounds composed of carbon, hydrogen, and oxygen in a ratio of about one carbon atom to two hydrogen atoms to one oxygen atom. The number of carbon atoms in a carbohydrate varies. Some carbohydrates serve as a source of energy. Other carbohydrates are used as structural materials. Carbohydrates can exist as monosaccharides, disaccharides, or polysaccharides. Monosaccharides A monomer of a carbohydrate is called a monosaccharide (MAHN-oh-SAK-uh-RIED). A monosaccharide—or simple sugar— contains carbon, hydrogen, and oxygen in a ratio of 1:2:1. The gen- eral formula for a monosaccharide is written as (CH2O)n, where n is any whole number from 3 to 8. For example, a six-carbon mono- saccharide, (CH2O)6, would have the formula C6H12O6. The most common monosaccharides are glucose, fructose, and galactose, as shown in Figure 3-6. Glucose is a main source of energy for cells. Fructose is found in fruits and is the sweetest of the monosaccharides. Galactose is found in milk. Notice in Figure 3-6 that glucose, fructose, and galactose have the same molecular formula, C6H12O6, but differing structures. The different structures determine the slightly different properties of the three compounds. Compounds like these sugars, with a single chemical formula but different structural forms, are called isomers (IE-soh-muhrz). SECTION 2 OBJECTIVES ● Distinguish between monosaccharides, disaccharides, and polysaccharides. ● Explain the relationship between amino acids and protein structure. ● Describe the induced fit model of enzyme action. ● Compare the structure and function of each of the different types of lipids. ● Compare the nucleic acids DNA and RNA. VOCABULARY carbohydrate monosaccharide disaccharide polysaccharide protein amino acid peptide bond polypeptide enzyme substrate active site lipid fatty acid phospholipid wax steroid nucleic acid deoxyribonucleic acid (DNA) ribonucleic acid (RNA) nucleotide C HO H C H OH C OH H C CH2OH H C H OH O Glucose C OH C O H OH C OH H CH2OH C H CH2OH Fructose C H HO C OH H C OH H C CH2OH H C H OH O Galactose Glucose, fructose, and galactose have the same chemical formula, but their structural differences result in different properties among the three compounds. FIGURE 3-6 Copyright © by Holt, Rinehart and Winston. All rights reserved. 56 CHAPTER 3 Disaccharides and Polysaccharides In living things, two monosaccharides can combine in a condensa- tion reaction to form a double sugar, or disaccharide (die-SAK-e-RIED). For example in Figure 3-4, the monosaccharides fructose and glu- cose can combine to form the disaccharide sucrose. A polysaccharide is a complex molecule composed of three or more monosaccharides. Animals store glucose in the form of the polysaccharide glycogen. Glycogen consists of hundreds of glucose molecules strung together in a highly branched chain. Much of the glucose that comes from food is ultimately stored in your liver and muscles as glycogen and is ready to be used for quick energy. Plants store glucose molecules in the form of the polysaccha- ride starch. Starch molecules have two basic forms—highly branched chains that are similar to glycogen and long, coiled, unbranched chains. Plants also make a large polysaccharide called cellulose. Cellulose, which gives strength and rigidity to plant cells, makes up about 50 percent of wood. In a single cellu- lose molecule, thousands of glucose monomers are linked in long, straight chains. These chains tend to form hydrogen bonds with each other. The resulting structure is strong and can be broken down by hydrolysis only under certain conditions. PROTEINS Proteins are organic compounds composed mainly of carbon, hydrogen, oxygen, and nitrogen. Like most of the other biological macromolecules, proteins are formed from the linkage of monomers called amino acids. Hair and horns, as shown in Figure 3-7a, are made mostly of proteins, as are skin, muscles and many biological catalysts (enzymes). Amino Acids There are 20 different amino acids, and all share a basic structure. As Figure 3-7b shows, each amino acid contains a central carbon atom covalently bonded to four other atoms or functional groups. A single hydrogen atom, highlighted in blue in the illustration, bonds at one site. A carboxyl group, —COOH, highlighted in green, bonds at a second site. An amino group, —NH2, highlighted in yel- low, bonds at a third site. A side chain called the R group, high- lighted in red, bonds at the fourth site. The main difference among the different amino acids is in their R groups. The R group can be complex or it can be simple, such as the CH3 group shown in the amino acid alanine in Figure 3-7b. The differences among the amino acid R groups gives different proteins very different shapes. The different shapes allow pro- teins to carry out many different activities in living things. Amino acids are commonly shown in a simplified way such as balls, as shown in Figure 3-7c. (a) Many structures, such as hair and horns are made of proteins. (b) Proteins are made up of amino acids. Amino acids differ only in the type of R group (shown in red) they carry. Polar R groups can dissolve in water, but nonpolar R groups cannot. (c) Amino acids have complex structures, so, in this and other textbooks, they are often simplified into balls. FIGURE 3-7 (b) Alanine (an amino acid) (c) Simplified version of amino acid CH3 H N OH C C H O H (a) Copyright © by Holt, Rinehart and Winston. All rights reserved. BIOCHEMISTRY 57 H H N C C OH H O H CH3 H2O Glycine Alanine H N OH C C H O H H H N C C H O H CH3 N OH C C H O H (a) (b) (a) The peptide bond (shaded blue) that binds amino acids together to form a polypeptide results from a condensation reaction that produces water. (b) Poly- peptides are commonly shown as a string of balls in this textbook and elsewhere. Each ball represents an amino acid. FIGURE 3-8 Substrate Products Enzyme 1 2 3 In the induced fit model of enzyme action, the enzyme can attach only to a substrate (reactant) with a specific shape. The enzyme then changes and reduces the activation energy of the reaction so reactants can become products. The enzyme is unchanged and is available to be used again. 3 2 1 FIGURE 3-9 Dipeptides and Polypeptides Figure 3-8a shows how two amino acids bond to form a dipeptide (die-PEP-TIED). In this condensation reaction, the two amino acids form a covalent bond, called a peptide bond (shaded in blue in Figure 3-8a) and release a water molecule. Amino acids often form very long chains called polypeptides (PAHL-i-PEP-TIEDZ). Proteins are composed of one or more polypep- tides. Some proteins are very large molecules, containing hun- dreds of amino acids. Often, these long proteins are bent and folded upon themselves as a result of interactions—such as hydrogen bonding—between individual amino acids. Protein shape can also be influenced by conditions such as temperature and the type of solvent in which a protein is dissolved. For exam- ple, cooking an egg changes the shape of proteins in the egg white. The firm, opaque result is very different from the initial clear, runny material. Enzymes Enzymes—RNA or protein molecules that act as biological catalysts—are essential for the functioning of any cell. Many enzymes are proteins. Figure 3-9 shows an induced fit model of enzyme action. Enzyme reactions depend on a physical fit between the enzyme molecule and its specific substrate, the reactant being catalyzed. Notice that the enzyme has folds, or an active site, with a shape that allows the substrate to fit into the active site. An enzyme acts only on a specific substrate because only that substrate fits into its active site. The linkage of the enzyme and substrate causes a slight change in the enzyme’s shape. The change in the enzyme’s shape weakens some chemical bonds in the substrate, which is one way that enzymes reduce activation energy, the energy needed to start the reaction. After the reaction, the enzyme releases the products. Like any catalyst, the enzyme itself is unchanged, so it can be used many times. An enzyme may not work if its environment is changed. For example, change in temperature or pH can cause a change in the shape of the enzyme or the substrate. If such a change happens, the reaction that the enzyme would have catalyzed cannot occur.

LARGE CARBON MOLECULES Many carbon compounds are built up from smaller, simpler molecules known as monomers (MAH-ne-mers), such as the ones shown in Figure 3-3. As you can also see in Figure 3-3, monomers can bond to one another to form polymers (PAWL-eh-mer). A polymer is a molecule that consists of repeated, linked units. The units may be identical or structurally related to each other. Large polymers are called macromolecules. There are many types of macromolecules, such as carbohydrates, lipids, proteins and nucleic acids. Monomers link to form polymers through a chemical reaction called a condensation reaction. Each time a monomer is added to a polymer, a water molecule is released. In the condensation reac- tion shown in Figure 3-4, two sugar molecules, glucose and fruc- tose, combine to form the sugar sucrose, which is common table sugar. The two sugar monomers become linked by a C—O—C bridge. In the formation of that bridge, the glucose molecule releases a hydrogen ion, H, and the fructose molecule releases a hydroxide ion, OH. The OH and H ions that are released then combine to produce a water molecule, H2O. In addition to building polymers through condensation reac- tions, living organisms also have to break them down. The break- down of some complex molecules, such as polymers, occurs through a process known as hydrolysis (hie-DRAHL-i-sis). In a hydrolysis reaction, water is used to break down a polymer. The water molecule breaks the bond linking each monomer. Hydrolysis is the reverse of a condensation reaction. The addition of water to some complex molecules, including polymers, under certain con- ditions can break the bonds that hold them together. For example, in Figure 3-4 reversing the reaction will result in sucrose breaking down into fructose and glucose. 2H2O Monomers Polymer C C O H OH C OH H CH2OH C H CH2OH C HO H C O H C OH H C CH2OH H C H OH O Sucrose C C O H OH C OH H CH2OH C H CH2OH C HO H C OH OH H C OH H C CH2OH H C H OH O Glucose Fructose H2O The condensation reaction below shows how glucose links with fructose to form sucrose. One water molecule is produced each time two monomers form a covalent bond. FIGURE 3-4 monomer from the Greek mono, meaning “single or alone,” and meros, meaning “a part” Word Roots and Origins A polymer is the result of bonding between monomers. In this example, each monomer is a six-sided carbon ring. The starch in potatoes is an example of a molecule that is a polymer. FIGURE 3-3 Copyright © by Holt, Rinehart and Winston. All rights reserved. 54 CHAPTER 3 ENERGY CURRENCY Life processes require a constant supply of energy. This energy is available to cells in the form of certain compounds that store a large amount of energy in their overall structure. One of these com- pounds is adenosine (uh-DEN-uh-SEEN) triphosphate, more commonly referred to by its abbreviation, ATP. The left side of Figure 3-5 shows a simplified ATP molecule struc- ture. The 5-carbon sugar, ribose, is represented by the blue carbon ring. The nitrogen-containing compound, adenine, is represented by the 2 orange rings. The three linked phosphate groups, —PO4 , are represented by the blue circles with a “P.” The phospate groups are attached to each other by covalent bonds. The covalent bonds between the phosphate groups are more unstable than the other bonds in the ATP molecule because the phosphate groups are close together and have negative charges. Thus, the negative charges make the bonds easier to break. When a bond between the phosphate groups is broken, energy is released. This hydrolysis of ATP is used by the cell to provide the energy needed to drive the chemical reactions that enable an organism to function.

Chapter 4 – ATOMIC STRUCTURE & CHEMICAL BONDING

Grade 9. Chapter-4. Atomic structure and chemical bonding

The plasma membrane (also called the cell membrane) has several functions. For example, it allows only certain molecules to enter or leave the cell. It separates internal metabolic reactions from the external environment. In addition, the plasma membrane allows the cell to excrete wastes and to interact with its environment. Membrane Lipids The plasma membrane, as well as the membranes of cell organelles, is made primarily of phospholipids. Phospholipids have a polar, hydrophilic (“water-loving”) phosphate head and two nonpolar, hydrophobic (“water-fearing”) fatty acid tails. Water molecules sur- round the plasma membrane. The phospholipids line up so that their heads point outward toward the water and their tails point inward, away from water. The result is a double layer called a phospholipid bilayer, as shown in Figure 4-10. The cell membranes of eukaryotes also contain lipids, called sterols, between the tails of the phospho- lipids. The major membrane sterol in animal cells is cholesterol. Sterols in the plasma membrane make the membrane more firm and prevent the membrane from freezing at low temperatures. SECTION 3 OBJECTIVES ● Describe the structure and function of a cell’s plasma membrane. ● Summarize the role of the nucleus. ● List the major organelles found in the cytosol, and describe their roles. ● Identify the characteristics of mitochondria. ● Describe the structure and function of the cytoskeleton. VOCABULARY phospholipid bilayer chromosome nuclear envelope nucleolus ribosome mitochondrion endoplasmic reticulum Golgi apparatus lysosome cytoskeleton microtubule microfilament cilium flagellum centriole Cell membranes are made of a phospholipid bilayer. Each phospholipid molecule has a polar “head” and a two-part nonpolar “tail.” FIGURE 4-10 Copyright © by Holt, Rinehart and Winston. All rights reserved. 78 CHAPTER 4 OUTSIDE OF CELL INSIDE OF CELL 1. Cell-surface marker: Glycoprotein that identifies cell type 3. Enzyme: Assists chemical reactions inside the cell 2. Receptor protein: Recognizes and binds to substances outside the cell 4. Transport protein: Helps substances move across cell membrane Carbohydrate portion Protein portion Phospholipid heads Phospholipid tails Phospholipid Cholesterol bilayer Membrane Proteins Plasma membranes often contain specific proteins embedded within the lipid bilayer. These proteins are called integral proteins. Figure 4-11 shows that some integral proteins, such as cell surface markers, emerge from only one side of the membrane. Others, such as receptor proteins and transport proteins, extend across the plasma membrane and are exposed to both the cell’s interior and exterior environments. Proteins that extend across the plasma membrane are able to detect environmental signals and transmit them to the inside of the cell. Peripheral proteins, such as the enzyme shown in Figure 4-11, lie on only one side of the membrane and are not embedded in it. As Figure 4-11 shows, integral proteins exposed to the cell’s external environment often have carbohydrates attached. These carbohydrates can act as labels on cell surfaces. Some labels help cells recognize each other and stick together. Viruses can use these labels as docks for entering and infecting cells. Integral proteins play important roles in actively transporting molecules into the cell. Some act as channels or pores that allow certain substances to pass. Other integral proteins bind to a mol- ecule on the outside of the cell and then transport it through the membrane. Still others act as sites where chemical messengers such as hormones can attach. Fluid Mosaic Model A cell’s plasma membrane is surprisingly dynamic. Scientists describe the cell membrane as a fluid mosaic. The fluid mosaic model states that the phospholipid bilayer behaves like a fluid more than it behaves like a solid. The membrane’s lipids and pro- teins can move laterally within the bilayer, like a boat on the ocean. As a result of such lateral movement, the pattern, or “mosaic,” of lipids and proteins in the cell membrane constantly changes.

Most of the functions of a eukaryotic cell are controlled by the nucleus, shown in Figure 4-12. The nucleus is filled with a jellylike liquid called the nucleoplasm, which holds the contents of the nucleus and is similar in function to a cell’s cytoplasm. The nucleus houses and protects the cell’s genetic information. The hereditary information that contains the instructions for the structure and function of the organism is coded in the organism’s DNA, which is contained in the nucleus. When a cell is not dividing, the DNA is in the form of a threadlike material called chromatin. When a cell is about to divide, the chromatin condenses to form chromosomes. Chromosomes are structures in the nucleus made of DNA and protein. The nucleus is the site where DNA is transcribed into ribonucleic acid (RNA). RNA moves through nuclear pores to the cytoplasm, where, depending on the type of RNA, it carries out its function. Nuclear Envelope The nucleus is surrounded by a double membrane called the nuclear envelope. The nuclear envelope is made up of two phos- pholipid bilayers. Covering the surface of the nuclear envelope are tiny, protein-lined holes, which are called nuclear pores. The nuclear pores provide passageways for RNA and other materials to enter and leave the nucleus. Nucleolus Most nuclei contain at least one denser area, called the nucleolus (noo-KLEE-uh-luhs). The nucleolus (plural, nucleoli) is the site where DNA is concentrated when it is in the process of making ribosomal RNA. Ribosomes (RIE-buh-SOHMZ) are organelles made of protein and RNA that direct protein synthesis in the cytoplasm. The nucleus of a cell is surrounded by a double membrane called the nuclear envelope. The nucleus stores the cell’s DNA. FIGURE 4-12 Nuclear envelope Nucleolus Nuclear pores DNA (chromatin) Copyright © by Holt, Rinehart and Winston. All rights reserved. 80 CHAPTER 4 MITOCHONDRIA Mitochondria (MIET-oh-KAHN-dree-uh) (singular, mitochondrion) are tiny organelles that transfer energy from organic molecules to adenosine triphosphate (ATP). ATP ultimately powers most of the cell’s chemical reactions. Highly active cells, such as muscle cells, can have hundreds of mitochondria. Cells that are not very active, such as fat-storage cells, have few mitochondria. Like a nucleus, a mitochondrion has an inner and an outer phos- pholipid membrane, as shown in Figure 4-13. The outer membrane separates the mitochondrion from the cytosol. The inner membrane has many folds, called cristae (KRIS-tee). Cristae contain proteins that carry out energy-harvesting chemical reactions. Mitochondrial DNA Mitochondria have their own DNA and can reproduce only by the division of preexisting mitochondria. Scientists think that mito- chondria originated from prokaryotic cells that were incorporated into ancient eukaryotic cells. This symbiotic relationship provided the prokaryotic invaders with a protected place to live and pro- vided the eukaryotic cell with an increased supply of ATP. RIBOSOMES Ribosomes are small, roughly spherical organelles that are respon- sible for building protein. Ribosomes do not have a membrane. They are made of protein and RNA molecules. Ribosome assembly begins in the nucleolus and is completed in the cytoplasm. One large and one small subunit come together to make a functioning ribosome, shown in Figure 4-14. Some ribosomes are free within the cytosol. Others are attached to the rough endoplasmic reticulum.

Related quizzes

Related quizzes