CH 106 Chemistry for Allied Health

1. Define monosaccharide, disaccharide, and polysaccharide.
2. Given the structure of a monosaccharide, identify the compound as an aldose or ketose.
3. Draw the linear structure and ring structure of glucose.
4. List three hexoses and one pentose that play important roles in human metabolism.
5. Define reducing sugar and explain, in terms of their structure, why lactose and maltose are reducing sugars and sucrose is not.
6. Describe the difference in the structures of starch, glycogen, and cellulose and explain why we can digest starch but not cellulose.
7. State the difference between (a) a simple and compound lipid, (b) a simple and mixed triacylglycerol, (c) a saturated and unsaturated fatty acid, and (d) a saponifiable and non-saponifiable lipid.
8. Define essential fatty acid.
9. Draw the general structure of a triacylglycerol, and write the equations for its hydrolysis and saponification.
10. Describe the process by which butter becomes rancid.
11. Given the iodine number of a lipid, describe the physical properties and most likely source of the lipid.
12. Explain how soap functions to remove grease from your hands.
13. Draw the general structure and describe the function of the following compound lipids: (a) phosphoglycerides, (b) sphingolipids, and (c) glycolipids.
14. Give three examples of non-saponifiable lipids.
15. Describe the components and structure of a cellular membrane.
16. Write the general structure of an amino acid.
17. State the difference between (a) a simple and a conjugated protein and (b) a globular and a fibrous protein.
18. Explain how an amino acid or a protein can act as a buffer.
19. Define zwitterion and isoelectric point.
20. Describe the differences and the types of bonding found in the primary, secondary, tertiary, and quaternary structure of proteins.
21. Define native state and denaturation.
22. State five methods for denaturing proteins.
23. Define metabolism and anabolic and catabolic reactions.
24. Identify the parts of an enzyme molecule.
25. Describe the method by which enzymes catalyze reactions.
26. Explain the lock-and-key and induced fit theories of enzyme action.
27. Explain how changes in ph and temperature will affect enzyme activity.
28. Define vitamin, and explain why vitamins are essential for normal cellular function.
29. Describe the function of hormones in the living organism.
30. Define multi-enzyme system, and explain how such systems are regulated.
31. Describe the ways in which enzyme activity can be inhibited, and give examples of each type of inhibition.
32. List the three components of nucleotides.
33. Name the sugars and bases found in DNA and RND.
34. Describe the structure of a DNA molecule and its method of replication.
35. List three types of RND, and describe their functions.
36. Describe the genetic code and its relationship to amino acids and polypeptide chains.
37. Describe the steps that occur in protein synthesis.
38. Define mutation, and indicate several ways, both positive and negative, in which mutations can affect the normal functions of an organism.

Statewide General Education Outcomes:

1. Gather, comprehend, and communicate scientific and technical information in order to explore ideas, models, and solutions and generate further questions.
2. Apply scientific and technical modes of inquiry, individually, and collaboratively, to critically evaluate existing or alternative explanations, solve problems, and make evidence-based decisions in an ethical manner.
3. Assess the strengths and weaknesses of scientific studies and critically examine the influence of scientific and technical knowledge on human society and the environment.

• Carbohydrates
  • Classes of carbohydrates
  • Photosynthesis
  • Monosaccharides
• Lipids
  • Fatty acids
  • Lipids containing fatty acids
  • Reactions of triacylglycerols
  • Tests for triacylglycerols
  • Phospholipids
  • Steroids and terpenes
• Proteins
  • Amino acids
  • Properties of amino acids
  • Essential amino acids
  • Peptide bonds
  • Protein structure
  • Functions of proteins
  • Denaturation of a protein
  • Testing for amino acids and proteins
• Enzymes and Digestion of Foodstuffs
  • Components of enzymes
  • Naming enzymes
  • Energy diagrams and catalysts
  • Enzymes as catalysts
  • Enzyme inhibition
  • Digestion of foodstuffs
• Metabolism: Energy Production in the Living Cell
  • The role of cellular structures and ATP in metabolism
  • The respiratory chain
  • Citric acid cycle
  • Oxidation of glucose
  • Oxidation of fatty acids and glycerol
  • Oxidation of amino acids
• Chemistry of Heredity: DNA and RNA. Recombinant DNA Technology and Modern Medicine selected Genetic Diseases.
  • Components of the nucleic acids
  • Structure of the nucleic acids
  • DNA replication
  • Protein synthesis
  • Cellular control
  • Recombinant DNA technology and modern medicine
  • Selected genetic diseases - e.g., PKU, Galactosemia, Tay-Sachs

Laboratory Content:

• Synthetic Polymers
  • Definition
  • Structure
  • Preparation
• Carbohydrates
  • Identification tests
  • Digestion and absorption
  • Alpha vs. beta D-glucose
• Lipids
  • Physical and chemical properties
  • Preparation and comparisons of soap
  • Water softening effects
• Nutrition
  • Iodide ion in salts
  • Calcium in milk
  • Phosphates in milk
  • Iron in breakfast cereals
• Proteins
  • Acid-base properties
  • Isoelectric point
  • Protein identification
  • Denaturation
  • Amino acids
• Enzymes
  • Chemical nature
  • Specificity
  • Substrate concentration
  • Temperature effect
  • pH effect
• Vitamin C
  • Content in fruit juices
  • Effect in heat on stability
• Urine
  • Properties
  • Investigation of “pathological” samples
• DNA and RNA
  • Replication of DNA
  • Transcription of DNA to mRNA
  • Translation of mRNA