Which of the following scenarios best illustrates the fundamental difference between active transport and passive transport in a cell membrane?

The movement of sodium ions against their concentration gradient using ATP, compared to the movement of water through aquaporins down its water potential gradient.

The use of protein carriers to move polar molecules down a gradient, compared to the use of protein channels to move ions against a gradient.

The secretion of enzymes via exocytosis, compared to the intake of fluid droplets through pinocytosis, both of which require no metabolic energy.

The movement of glucose through a symporter using a pre-existing electrochemical gradient, compared to the simple diffusion of carbon dioxide through the lipid bilayer.

A researcher observes a cell utilizing a membrane protein to move Ca^{2+} ions from the cytosol, where the concentration is 10^{-7} M , to the endoplasmic reticulum, where the concentration is 10^{-3} M . Which statement correctly categorizes this process and the energy requirement?

It is active transport because the ions are moving against their concentration gradient, requiring ATP hydrolysis.

It is facilitated diffusion because a membrane protein is involved, meaning no metabolic energy is required.

It is passive transport because the small size of the calcium ions allows them to move through the bilayer without energy.

It is secondary active transport because it relies on the kinetic energy of the ions rather than chemical energy.

Which of the following describes a characteristic shared by both facilitated diffusion and primary active transport?

Both processes require the use of specific membrane-spanning proteins to facilitate the movement of molecules.

Both processes result in the net movement of substances from an area of high concentration to an area of low concentration.

Both processes utilize the hydrolysis of ATP to provide the necessary energy for solute translocation.

Both processes are independent of the solubility of the molecule in the hydrophobic core of the lipid bilayer.

Which of the following transport mechanisms is correctly paired with its driving force and effect on the cell's electrochemical gradient?

The sodium-potassium pump uses ATP to maintain a membrane potential by moving three Na^{+} out and two K^{+} into the cell.

Simple diffusion uses membrane proteins to move nonpolar molecules like O_{2} from areas of low partial pressure to high partial pressure.

Facilitated diffusion of glucose uses ATP to accelerate the movement of sugars into the cell regardless of the external concentration.

Osmosis uses the kinetic energy of water molecules to move solutes against their concentration gradient to achieve isotonicity.

An artificial cell with a 0.5 M glucose internal concentration is placed in a beaker containing a 0.1 M glucose solution. If the membrane is permeable to glucose but the cell continues to take in glucose molecules via a membrane protein, which of the following is the most likely classification of this transport and its requirement?

Active transport, because the cell is moving glucose from an area of low concentration to high concentration, requiring ATP.

Secondary active transport, because the movement of glucose is being powered by the osmotic pressure of the surrounding water.

Facilitated diffusion, because the glucose is moving through a membrane protein down its concentration gradient.

Passive transport, because the movement of glucose will naturally continue until dynamic equilibrium is reached at 0.3 M.

Which of the following transport mechanisms would be most affected by a drug that inhibits the production of cellular ATP by the mitochondria?

The movement of H^{+} ions across a membrane to establish a proton gradient.

The movement of water molecules through aquaporin channels into a hypertonic cell.

The movement of ethanol across the phospholipid bilayer according to its concentration gradient.

The movement of CO_{2} out of the cell down its partial pressure gradient.

Which of the following describes a key difference between primary active transport and facilitated diffusion regarding the saturation of transport proteins?

Both processes can reach a maximum rate of transport (Vmax) when all membrane proteins are occupied, but only primary active transport can maintain a concentration gradient where C_{inside} \neq C_{outside} at equilibrium.

Only facilitated diffusion is selective for specific solutes, whereas active transport pumps can move any charged ion across the membrane regardless of size.

Primary active transport moves molecules down their electrochemical gradient until the concentrations are equal, while facilitated diffusion moves them against the gradient.

Facilitated diffusion requires the phosphorylation of the carrier protein to change shape, whereas active transport proteins change shape spontaneously.

Which of the following observations would provide the strongest evidence that a specific amino acid is entering a cell via secondary active transport rather than facilitated diffusion?

The movement of the amino acid into the cell ceases when the Na^{+} electrochemical gradient across the membrane is dissipated, even if ATP levels remain high.

The transport process requires the direct hydrolysis of one ATP molecule for every amino acid molecule that crosses the membrane.

The rate of amino acid entry increases linearly as the external concentration of the amino acid increases, without ever reaching a maximum rate.

The amino acid is a polar molecule and is observed moving through a protein channel down its concentration gradient.

A biologist identifies a protein in the plasma membrane that moves K^{+} ions into the cell while simultaneously moving Na^{+} ions out of the cell. If the internal concentration of K^{+} is much higher than the external concentration, which of the following best describes this mechanism?

Active transport, because it uses energy to move ions against their respective concentration gradients to maintain a non-equilibrium state.

Passive transport, because the simultaneous movement of two different ions cancels out the need for metabolic energy.

Simple diffusion, because the small size of the ions allows them to pass through the hydrophobic tails of the phospholipids.

Facilitated diffusion, because the ions are moving through a protein channel to reach dynamic equilibrium.

Which of the following scenarios describes a primary active transport mechanism rather than a facilitated diffusion process?

A membrane protein hydrolyzes ATP to pump Ca^{2+} ions out of the cytosol into the extracellular fluid where the concentration of Ca^{2+} is 1,000 times higher.

Aquaporins provide a hydrophilic path for water molecules to move rapidly into a cell placed in a hypotonic solution.

A carrier protein changes shape to move glucose molecules into a muscle cell from a region of high blood sugar to a region of lower internal concentration.

A channel protein allows Cl^{-} ions to flow out of a cell following their electrochemical gradient until equilibrium is reached.

Distinguish active vs passive transport

Distinguish active from passive voice.

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.

Life Processes Identify and define the seven life processes (MRS GREN). Classification Group living organisms based on observed similarities and differences. Classify vertebrates into taxonomic groups based on visible physical characteristics. Construct a dichotomous key to classify vertebrates. Cells Compare the structure of generalised plant and animal cells, and selected microbes (e.g. bacteria, fungi and Amoeba) Distinguish among cell wall, cell membrane, nucleus, cytoplasm, temporary and permanent vacuoles, mitochondrion, chloroplast, endoplasmic reticulum and ribosomes. Relate the structure of organelles to their functions; Identify specialised cells such as blood cells, ciliated epithelial cells, nerve cells, root hair cells, sperm cells and egg cells. Explain the importance of cell specialisation in multicellular organisms; include hierarchy of cells, tissues, organs; organ systems and then organism Diffusion, Osmosis, Active transport and Osmoregulation Explain the processes of diffusion, osmosis and active transport. Identify everyday instances of these processes occurring. Discuss the importance of diffusion, osmosis and active transport in living systems. Nutrition in Plants Describe the process of photosynthesis in green plants; test for end products, starch or reducing sugar (glucose). Relate the structure of the leaf of a flowering plant to its function in photosynthesis; draw and label the external features and the internal structure (cross section) of a leaf as seen in cross section under the light microscope. Nutrition in Humans Discuss the importance of a balanced diet in humans. State components of a balanced diet (carbohydrates, fats, proteins, vitamins and minerals, water and roughage and their roles) along with the results of their deficiency or surplus. Suggest dietary recommendations for treating and preventing named deficiency and physiological diseases (such as those outlined in the manual and your notes). Perform tests to distinguish among food substances - Test for proteins (Biuret), fats (grease spot), starch (iodine), reducing sugars (Benedict’s solution). The Digestive System in Humans Relate the structures of the human alimentary canal to their functions; Draw and label simple diagrams of the alimentary canal and internal structure of a tooth required. Describe mastication and the role of teeth in the mechanical breakdown of food to be included. (Compare types of teeth in humans and compare types of teeth in herbivores and carnivores.) Explain the role and importance of enzymes role of digestive enzymes in the mouth, stomach and pancreatic enzymes in the small intestine. Discuss properties of enzymes. Deduce from tables and graphs the effects of temperature and pH on enzyme activity. Experimental Skills Follow all drawing rules as outlined in the drawing skills checklist posted in the classroom (including calculation of magnification).

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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