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The Chemistry of Life 2. List four characteristics of water that are emergent properties resulting from hydrogen bonding. 3. Define cohesion and adhesion. Explain how water’s cohesion and adhesion contribute to the movement of water Elements and compounds from the roots to the leaves of a tree. 4. Explain the following observations by referring to the 1. Distinguish between an element and a compound. properties of water: 2. Identify the four elements that make up 96% of living matter. Coastal areas have milder climates than adjacent inland Atoms and molecules areas. Ocean temperatures fluctuate much less than 3. Draw and label a simplified model of an atom. temperatures on land. 4. Explain how the atomic number and mass number of an Insects like water striders can walk on the surface of a atom can be used to determine the number of neutrons. pond without breaking the surface. 5. Explain how two isotopes of an element are similar. If you slightly overfill a water glass, the water will form a Explain how they are different. convex surface above the top of the glass. 6. Describe a biological application that uses radioactive If you place a paper towel so that it touches spilled water, isotopes. the towel will draw in the water. Electron distribution and chemical properties Ice floats on water. Humans sweat and dogs pant to cool themselves on hot 7. Define the terms energy and potential energy. Explain days. why electrons in the first electron shell have less potential The Solvent of Life energy than electrons in higher electron shells. CHAPTER 2 THE CHEMICAL CONTEXT OF LIFE Learning objectives: 8. Distinguish between nonpolar covalent, polar covalent and ionic bonds. 9. Explain why strong covalent bonds and weak bonds are both essential in living organisms. 10. Give an example that illustrates how a molecule’s shape can determine its biological function. CHAPTER 3 WATER AND THE FITNESS OF THE ENVIRONMENT Learning objectives: The Properties of Water 1. With the use of a diagram or diagrams, explain why water molecules are: a. polar b. capable of hydrogen bonding with 4 neighboring water molecules 5. Distinguish between a solute, a solvent and a solution. 6. Distinguish between hydrophobic and hydrophilic substances. The Dissociation of Water Molecules 7. Name the products of the dissociation of water and give their concentration in pure water. 8. Define acid, base, and pH. 9. Explain how acids and bases may directly or indirectly alter the hydrogen ion (H+) concentration of a solution. 10. Using the bicarbonate buffer system as an example, explain how buffers work. CHAPTER 4 CARBON AND THE MOLECULAR DIVERSITY OF LIFE Learning objectives: The Importance of Carbon 1. Explain how carbon’s electron configuration explains its ability to form large, complex and diverse organic molecules. 2. Describe the basic structure of a hydrocarbon and explain why these molecules are hydrophobic. Chemical Groups 3. Name the major chemical groups found in organic molecules. Describe the basic structure of each chemical group and outline the chemical properties of the organic molecules in which they occur. ATP 4. Explain how ATP functions as the primary energy transfer molecule in living cells. CHAPTER 5 THE STRUCTURE AND FUNCTION OF LARGE BIOLOGICAL MACROMOLECULES Learning objectives: The Molecules of Life 1. List the four major classes of macromolecules. 2. Distinguish between monomers and polymers. 3. Draw diagrams to illustrate condensation and hydrolysis reactions. Carbohydrates Serve as Fuel and Building Material 4. Distinguish between monosaccharides, disaccharides, and polysaccharides. 5. Describe the formation of a glycosidic linkage. 6. Distinguish between the glycosidic linkages found in starch and cellulose. Explain why the difference is biologically important. Lipids are a Diverse Group of Hydrophobic Molecules 7. Describe the building-block molecules, structure, and biological importance of fats, phospholipids, and steroids. 8. Identify an ester linkage and describe how it is formed. 9. Distinguish between saturated and unsaturated fats. 10. Name the principal energy storage molecules of plants and animals. Proteins have Many Structures, Resulting in a Wide Range of Functions 11. Distinguish between a protein and a polypeptide. 12. Explain how a peptide bond forms between two amino acids. 13. List and describe the four major components of an amino acid. Explain how amino acids may be grouped according to the physical and chemical properties of the R group. 14. Explain what determines protein structure and why it is important. 15. Explain how the primary structure of a protein is determined. 16. Name two types of secondary protein structure. Explain the role of hydrogen bonds in maintaining secondary structure. 17. Explain how weak interactions and disulfide bridges contribute to tertiary protein structure. 18. List four conditions under which proteins may be denatured. Nucleic Acids Store and Transmit Hereditary Information 19. List the major components of a nucleotide, and describe how these monomers are linked to form a nucleic acid. 20. Distinguish between: a. pyrimidine and purine b. nucleotide and nucleoside c. ribose and deoxyribose d. 5 end and 3 end of a nucleotide 21. Briefly describe the three-dimensional structure of DNA. CHAPTER 8 AN INTRODUCTION TO METABOLISM Learning objectives: Metabolism, Energy, and Life 1. Explain the role of catabolic and anabolic pathways in cellular metabolism. 2. Distinguish between kinetic and potential energy. 3. Explain why an organism is considered an open system. 4. Explain the first and second laws of thermodynamics in your own words. 5. Distinguish between exergonic and endergonic reactions in terms of free energy change. 6. List the three main kinds of cellular work. Explain in general terms how cells obtain the energy to do cellular work. 7. Describe the structure of ATP and identify the major class of macromolecules to which ATP belongs. 8. Explain how ATP performs cellular work. Protein Enzymes Regulate Metabolic Pathways 9. Describe the function of enzymes in biological systems. 10. Explain why an investment of activation energy is necessary to initiate a reaction. 11. Explain how enzyme structure determines enzyme specificity. 12. Explain the induced-fit model of enzyme function. 13. Explain how substrate concentration affects the rate of an enzyme-catalyzed reaction. 14. Explain how temperature, pH, cofactors, and enzyme inhibitors can affect enzyme activity. The Control of Metabolism 15. Describe how allosteric regulators may inhibit or stimulate the activity of an enzyme. 16. Explain how feedback inhibition prevents a cell from wasting chemical resources. KEY VOCABULARY: Ch. 2: The Chemical Context of Life 1. Element 2. Compound 3. Atom 4. Atomic number 5. Isotopes Ch. 3: Water and the Fitness of the Environment 1. Cohesion 2. Adhesion 3. Surface tension 4. Specific heat 5. Heat of vaporization Ch. 4: Carbon and the Molecular Diversity of Life 1. Organic chemistry 2. Hydrocarbons 3. Isomers 4. Functional groups 5. Hydroxyl group Ch. 5: The Structure and Function of Large Biological Molecules 1. Polymer 2. Monomer 3. Condensation reaction (dehydration reaction) 4. Hydrolysis 5. Enzymes Ch. 8: An Introduction to Metabolism 1. Metabolism 2. Kinetic energy 3. Potential energy 4. Exergonic reaction 5. Endergonic reaction 6. 7. 8. 9. 10. Electron shell Nonpolar covalent bond Polar covalent bond Ionic bond Hydrogen bond 6. 7. 8. 9. 10. Hydrophilic Hydrophobic Hydronium ion Hydroxide ion Buffer 6. 7. 8. 9. 10. Carbonyl group Carboxyl group Amino group Phosphate group Adenosine triphosphate (ATP) 6. 7. 8. 9. 10. Carbohydrates Lipids Proteins Denaturation Nucleic acids 6. 7. 8. 9. 10. Energy coupling Activation energy Substrate Active site Feedback inhibition CHAPTER REVIEW QUESTIONS (CRQ): Chapter 2: The Chemical Context of Life 1. Briefly describe each subatomic particle (proton, neutron, electron) with regard to its location and charge. 2. How are covalent bonds formed? Identify and differentiate between the two types of covalent bonds. 3. How are ionic bonds formed? Differentiate between a cation and an anion. 4. What are hydrogen bonds and why are weak bonds important in biology? Chapter 3: Water and the Fitness of the Environment 1. Differentiate between cohesion and adhesion. Provide an example of each with regards to water. 2. How does water moderate air temperature on Earth? 3. Why does ice float and what significance does this have for organisms that live in aquatic environments? 4. Explain why water is the most versatile solvent, but is not a universal solvent. 5. How does dissociation of water molecules affect the pH of a solution? Chapter 4: Carbon and Molecular Diversity of Life 1. Describe (atomic number, # of p+/e-, arrangement of e-) and draw the electron dot diagram of a carbon atom. 2. What type of bond does carbon almost always form with other atoms? Why? 3. Answer each with the correct functional group: o Which functional group of organic molecules is a proton donor? Would a solution containing this type of molecule be acidic or basic? o Which functional group tends to form a base in water? o Which functional group usually has a -2 charge when dissolved in water? 4. Why are functional groups important in biology? Chapter 5: The Structure and Function of Macromolecules 1. Explain what is meant by condensation/dehydration synthesis. What is the opposite process called? How are both important to most biological molecules? 2. Differentiate between the following polysaccarides: starch, glycogen, cellulose and chitin. 3. Distinguish between a saturated fat and an unsaturated fat. Which type of fat is most common in animal tissue? 4. Describe the general structure of phospholipids, and explain why their structure relates to their function in cell membranes. 5. Describe the four levels of organization possible in a protein, and explain what forces are involved at each level. What must a protein have in order to have a quartenary structure? 6. What is denaturation? How or when may it occur? What happens to a polypeptide/protein when it becomes denatured? Chapter 8: An Introduction to Metabolism 1. Draw and label the three components of an ATP molecule. 2. In an ATP molecule, which bond is likely to break? By what chemical mechanism is the bond broken? Why does the reaction described above release so much energy? 3. How does ATP power cellular work? 4. Draw and label a graph depicting the progress of an exergonic reaction with and without an enzyme catalyst. 5. What is energy of activation and what does it have to do with chemical reactions? How does an enzyme affect the energy of activation?