Chapters 4~5: Biochemistry
AP Biology
Stoneleigh-Burnham School
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Judith S. de Nuño
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Chapter Objectives

1. Summarize the philosophies of vitalism and mechanism
2. Explain how vitalism and mechanism influenced the devellpment of organic chemistry and biology
3. Explain how carbon's electron configuration determines the kinds and number of bonds carbon will form
4. Describe how carbon skeletons may vary
5. Explain how the variation in carbon skeleton contributes to the diversity and complexity of organic      molecules
6. Distinguish among the three types of isomers: structural, geometric, and enantiomers
7. Recognize and identify the structural formulas for the major functional groups and describe the chemical properties of organic molecules in which they occur
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8. List the 4 major classes of biomolecules
9. Explain how organic polymers contribute to biological diversity
10. Describe how covalent linkages are formed and broken in organic polymers
11. Describe the distinguishing characteristics of carbohydrates and explain how they are classified
12. List four characteristics of a sugar and identify the structural formulas of representative mono- and      disaccharides
13. Identify a glycosidic linkage and describe how it is formed
14. Describe the important biological functions of polysaccharides
15. Distinguish between the glycosidic linkages found in starch and cellulose and explain wh the       difference is biologically important
16. Explain what distinguishes lipids from other major classes of macromolecules
17. Identify an ester linkage and describe how it is formed
18. Distintuish between saturated and unsaturated fats and steroid-based lipids and identify the formulas for representative examples
19. Describe the characteristics that distinguish proteins from the other major classes of macromolecules and explain the biologically important functions of proteins
20. Lilst and recognize four components of and amino acid and explain how amino acids may be grouped according to the physical and chemical properties of the side chains
21. Identify the structural formulas of biologically important amino acids
22. Identify a peptide bond and explain how it is formed
23. Explain what determines protein conformation and why it is important
24. Define primary structure and describe how it may be deduced in the laboratory
25. Describe the two types of secondary protein structure and explain the role of hydrogen bonds in       maintaining the structure
26. Explain how weak interactions and disulfide bridges contribute to tertiary protein structure
27. Using collagen and hemoglobin as examples, describe quartenary protein structure
28. Define denaturation and explain how proteins my be denatured
29. Describe the characteristics that distinguish nucleic acids from the othe rmajor groups of       macromolecules
30. Summarize the functions of nucleic acids
31. List the components of a nucleotide and describe how these monomers are linked togehter to from a nucleic acid
32. Recognize and distinguish between the structural formula of purine and pyrimidine bases
33. Distinguish between the structural formulas of ribose and dexoyribose
34. List the functions of nucleotides
35. Briefly describe the 3-dimenstional structure of DNA

Chapter Terms:

  • organic chemistry
  • hydrocarbon
  • isomer
  • structural isomer
  • geometric isomer
  • enantiomer
  • functional group
  • hydroxyl group
  • alcohol
  • carbonyl group
  • ketone
  • aldehyde
  • carboxyl group
  • carboxylic acid
  • amino group
  • amine
  • sulfhydryl group
  • thiol
  • phosphate group
  • polymer
  • monomer
  • condensation reaction
  • dehydration reaction
  • hydrolysis
  • carbohydrate
  • monosaccharide
  • disaccharide
  • glycosidic linkage
  • polysaccharide
  • starch glycogen
  • double helix
  • cellulose
  • chitin
  • lipid
  • fat
  • fatty acid
  • triacylglycerol
  • saturated fatty acid
  • unsaturated fatty acid
  • steroid
  • cholesterol
  • protein
  • conformation
  • polypeptide
  • amino acid
  • protein
  • peptide bond
  • primary structure
  • secondary structure
  • alpha helix
  • pleated sheet
  • tertiary structure
  • hydrophobic interaction
  • disulfide bridges
  • quarternary structure
  • denaturation
  • chaperone proteins
  • gene
  • nucleic acid
  • deoxyribonucleic acid
  • ribonucleic acid
  • nucleotide
  • pyrimidine
  • purine
  • ribose
  • deoxyribose
  • polynucleotide

 

Chapter Outline Framework

A. The Importance of Carbon

1. Organic chemistry is the study of carbon compounds
2. Carbon atoms are the most versatile building blocks of molecules
3. Variation in carbon skeletons contributes to the diversity of organic molecules

B. Functional Groups

1. Functional groups also contribute to the molecular diversity of life

a. hydroxyl group and alcohols
b. carbonyl group and aldehydes and ketones
c. carboxyl group and carboxylic acids
d. amion groups and amines
e. sulfhydryl group and thiols
f. phosphate groups

C. Polymer Principles

1. Most macromolecules are polymers
2. A limitless variety of polymers can be built from a small set of monomers

D. Carbohydrates: Fuel and Building Material

1. Sugars

a. smallest carbohydrates
b. serve as fuel and carbon sources

2. Polysaccharides

a. polymers made of sugars
b. storage and structure

E. Lipids: Diverse Hydrophobic Molecules

1. Fats store large amounts of energy
2. Phospholipids are major components of cell membranes
3. Steroids include cholesterol and certain hormones

F. Proteins: The Molecular Tools of the Cell

1. A polypeptide is a polymer of amino acids connected in a specific sequence
2. A protein's function depends on its specific conformation

G. Nucleic Acids: Informational Polymers

1. Nucleic acids store and transmit hereditary information
2. A nucleic acid strand is a polymer of nucleotides
3. Inheritance is based on replication of the DNA double helix
4. DNA and proteins can serve as tape measures of evolution

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