Someone that is pro-business would....

take all the money from businesses

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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.

In many cases, cells must move materials from an area of lower concentration to an area of higher concentration, or “up” their concentration gradient. Such movement of materials is known as active transport. Unlike passive transport, active transport requires a cell to expend energy. CELL MEMBRANE PUMPS Ion channels and carrier proteins not only assist in passive trans- port but also help with some types of active transport. The car- rier proteins that serve in active transport are often called cell membrane “pumps” because they move substances from lower to higher concentrations. Carrier proteins involved in facilitated diffusion and those involved in active transport are very similar. In both, the molecule first binds to a specific kind of carrier protein on one side of the cell membrane. Once it is bound to the molecule, the protein changes shape, shielding the molecule from the hydrophobic interior of the phospholipid bilayer. The protein then transports the molecule through the membrane and releases it on the other side. However, cell membrane pumps require energy. Most often the energy needed for active transport is supplied directly or indirectly by ATP. Sodium-Potassium Pump One example of active transport in animal cells involves a carrier protein known as the sodium-potassium pump. As its name sug- gests, this protein transports Na ions and K ions up their con- centration gradients. To function normally, some animal cells must have a higher concentration of Na ions outside the cell and a higher concentration of K ions inside the cell. The sodium- potassium pump maintains these concentration differences. Follow the steps in Figure 5-6 on the next page to see how the sodium-potassium pump operates. First, three Na ions bind to the carrier protein on the cytosol side of the membrane, as shown in step . At the same time, the carrier protein removes a phosphate group from a molecule of ATP. As you can see in step , the phos- phate group from the ATP molecule binds to the carrier protein. Step shows how the removal of the phosphate group from ATP supplies the energy needed to change the shape of the carrier pro- tein. With its new shape, the protein carries the three Na ions through the membrane and then forces the Na ions outside the cell where the Na concentration must remain high. 3 2 1 SECTION 2 OBJECTIVES ● Distinguish between passive transport and active transport. ● Explain how the sodium-potassium pump operates. ● Compare endocytosis and exocytosis. VOCABULARY active transport sodium-potassium pump endocytosis vesicle pinocytosis phagocytosis phagocyte exocytosis www.scilinks.org Topic: Active Transport Keyword: HM60018 mb06se_homs02.qxd 5/18/07 11:02 AM Page 103 104 CHAPTER 5 K+ K+ K+ K+ K+ K+ INSIDE OF CELL OUTSIDE OF CELL Carrier protein Cell membrane P P P P Na+ Na+ Na+ ATP ADP Na+ Na+ Na+ Na+ Na+ Na+ 1 2 3 4 5 6 At this point, the carrier protein has the shape it needs to bind two K ions outside the cell, as step shows. When the K ions bind, the phosphate group is released, as indicated in step , and the carrier protein restores its original shape. As shown in step this time, the change in shape causes the carrier protein to release the two K ions inside the cell. At this point the carrier protein is ready to begin the process again. Thus, a complete cycle of the sodium-potassium pump transports three Na ions out of the cell and two K ions into the cell. At top speed, the sodium-potassium pump can transport about 450 Na ions and 300 K ions per second. The exchange of three Na ions for two K ions creates an electrical gradient across the cell membrane. That is, the outside of the membrane becomes positively charged relative to the inside of the membrane, which becomes relatively negative. In this way, the two sides of the cell membrane are like the positive and nega- tive terminals of a battery. This difference in charge is important for the conduction of electrical impulses along nerve cells. The sodium-potassium pump is only one example of a cell membrane pump. Other pumps work in similar ways to transport important metabolic materials across cell membranes.

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.

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Pro-Start Foundations of Restaurant Management Level 1

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