[IB Biology at GHS: Chemistry of Life]


Course Objectives for IB Biology

Gresham HS

Topic Two: Chemistry of Life


Reading:

Chapter 2- Basic Chemistry

Chapter 3- Organic Chemistry

Chapter 8- Enzymes

Chapter 14- DNA: The Genetic Material

Chapter 15- Genes and How They Work

Chapter 16- Control of Gene Expression

Chapter 18- Gene Technology


2.1 Elements of life (2 hours) (pp. 19-34)

2.1.1 State that the 3 commonest elements of life are carbon, hydrogen and oxygen. (pg. 25)

2.1.2 State that a variety of other elements are needed by living organisms including nitrogen, sulfur, phosphorus, iron and potassium. (pg. 25)

2.1.3 State one role for each of the elements (in plant or animals) mentioned in 2.1.2. (pg. 25)

2.1.4 Outline the difference between an atom and an ion. (Ions only in terms of being charged particles.) (pg. 26)

2.1.5 Define organic. (pg. 38)

2.1.6 Outline the significance of water in biology including transparency, cohesion, surface tension, solvent properties and thermal properties, referring to the polarity of water molecules and hydrogen bonding where relevant. (One example of each is sufficient.) (pp. 28-33)

2.1.7 Discuss the significance of water to organisms (in plant or animals) as a coolant, transport medium and habitat, in terms of its properties. (pp. 28-33)


2.2 Carbohydrates, lipids and proteins (4 hours) (pp. 38-55)

2.2.1 Draw the basic structure of a generalized amino acid. (pp. 50-51)

2.2.2 Draw the ring structure of alpha-D-glucose. (pg. 44)

2.2.3 Draw the basic structure of glycerol and a generalized fatty acid. (pp. 46-47)

2.2.4 Outline the role of condensation and hydrolysis in the relationships between monosaccharides and disaccharides; fatty acids, glycerol and triglycerides; amino acids, dipeptides and polypeptides. (pg. 50)

2.2.5 Draw the structure of a generalized dipeptide, showing the peptide linkage. (pg. 50)

2.2.6 Explain the relative solubility of carbohydrates, lipids and protein in water. (This is easy to try on your own at home!)

2.2.7 Compare the energy content of carbohydrates, lipids and proteins. (pg. 46)

2.2.8 List 2 examples each of monosaccharides, disaccharides and one for a polysaccharide. (pg. 40)

2.2.9 State 1 function for a monosaccharide and 1 for a polysaccharide. (pg. 40)

2.2.10 State 3 functions of lipids. (pp. 45-47)


8.5 Proteins (1 hour) (pp. 48-55)

8.5.1 Explain the four levels of structure of proteins, indicating their significance (primary, secondary, tertiary, quaternary). (pp. 52-55)

8.5.2 Outline the difference between fibrous and globular proteins, with reference to two examples of each type. (fibrous ?, globular pp. 52-55)

8.5.3 State six functions of proteins, giving a named example of each. (pp. 48-49)


2.3 Enzymes (4 hours) (pp. 148-154)

2.3.1 Define enzyme. (pp. 150-151)

2.3.2 Define active site. (pg. 151)

2.3.3 Describe the "lock-and-key" model. (pg. 151)

2.3.4 List 3 factors that affect enzyme activity (include at least temp. and substrate concentration). (pg. 152)

2.3.5 Outline the effects of temperature and substrate concentration on enzyme activity. (pg. 152)

2.3.6 Define denaturation. (pg. 55)

2.3.7 Explain 2 applications of enzymes in biotechnology.

8.6.1 State that metabolic pathways consist of chains and cycles of enzyme catalyzed reactions.

8.6.2 Describe the "induced fit" model. (Include its importance in the reduction of the activation energy and how it can account for the broad specificity of some enzymes (ability to bind several substrates).) (pg. 151)

8.6.3 Explain that enzymes lower the activation energy of the chemical reactions that they catalyze. (Graphically cover both exergonic and endergonic reactions. An understanding of how to calculate the activation energy of a reaction when reversed is also needed.) (pp. 148-149)

8.6.4 Explain the difference between competitive and non-competitive inhibition, with reference to one example of each type. (pg. 152)

8.6.5 Explain the role of allostery with respect to feedback inhibition and the control of metabolic pathways. (pg. 152)


2.4 DNA structure (1 hour)

2.4.1 Outline DNA nucleotide structure in terms of sugar (deoxyribose), base and phosphate. (pp. 56-57)

2.4.2 State the names of the four bases in DNA. (pg. 57)

2.4.3 Outline how the DNA nucleotides are linked together by covalent bonds into a single strand. (pg. 57)

2.4.4 Explain how a DNA double helix is formed using complementary base pairing and hydrogen bonds. (pg. 58)

2.4.5 Draw a simple diagram of the molecular structure of DNA. (pg. 56-58)


8.1 DNA Structure (1 hour)

8.1.1 Outline the structure of nucleosomes including histone proteins and DNA (Limit the discussion to the fact that a nucleosome consists of 8 small histone protein molecules wrapped around with DNA and held together by another histone protein.). (pp. 89, 208-209, 327)

8.1.2 State that only a small proportion of the DNA in the nucleus constitutes genes and that the majority consists of repetitive sequences (See 8.3.4.). (The function of these repetitive sequences is not required but students should know that their presence is used in profiling.) (pg. 310)

8.1.3 Explain the structure of DNA including the antiparallel strands, 3'-5' linkages and hydrogen bonding between purines and pyrimidines. (pp. 286-287)


2.5 DNA replication (1 hour)

2.5.1 State that DNA replication is semi-conservative. (pg. 288)

2.5.2 Outline DNA replication in terms of unwinding the double helix and separation of the strands by helicase followed by formation of the new complementary strands by DNA polymerase. (pp. 290-293)

2.5.3 Explain the significance of complementary base pairing in the conservation of the base sequence of DNA. (pp. 286-287)


8.2 DNA replication (1 hour)

8.2.1 State that DNA replication is carried out in a 5'----->3' direction. (pp. 290-291)

8.2.2 Explain the process of DNA replication in eukaryotes including the role of enzymes (helicase, DNA polymerase III, RNA primase, DNA polymerase I and DNA ligase), Okazaki fragments and deoxynucleoside triphosphates. (The function of the enzymes should be stated in general terms only. The explanation of the Okazaki fragments in relation to the direction of action of DNA Polymerase III is required.) (pp. 290-293)

8.2.3 State that in an eukaryotic chromosome, replication is initiated at many points. (pg. 291)


2.6 Transcription and translation (2 hours)

2.6.1 Compare the structure of RNA and DNA. (Limit it to names of sugars, bases and number of strands.) (pg. 58)

2.6.2 State one function of messenger RNA and one function of transfer RNA. (pg. 300)

2.6.3 Outline DNA transcription in terms of the formation of a RNA strand complementary to the DNA strands by RNA polymerase. (pg. 301)

2.6.4 Describe the genetic code in terms of codons composed of triplets of bases. (pg. 302-303)

2.6.5 Describe translation including the roles of mRNA codons, t RNA anticodons and ribosomes leading to peptide linkage formation. (pp. 306-309)

2.6.6 Define the terms degeneracy and universal as they relate to the genetic code.

2.6.7 Explain the relationship between one gene and one polypeptide and its significance.


8.3 Transcription (2 hours)

8.3.1 State that transcription is carried out in a 5'---->3' direction. (pg. 304)

8.3.2 Outline the Lac Operon model as an example of the control of gene expression in prokaryotes. (Operons are only found in prokaryotes. Mention only the idea of a regulator gene producing a protein that prevents RNA polymerase binding to the promoter region.) (pp. 322-323)

8.3.3 Explain the process of transcription in eukaryotes including the role of the promoter region, RNA polymerase, ATP, and terminator. (See IB syllabus for further details.) (pg. 304-305)

8.3.4 State that eukaryotic chromosomes contain far more DNA than is needed to code for their protein products (See 8.1.2.). (pg. 310)

8.3.5 Outline the difference between introns and exons. (pg. 310)

8.3.6 State that eukaryotic RNA needs the removal of introns to form mature mRNA and that this process is called splicing.

8.3.7 State that a small group of viruses, known as retroviruses, cause host cells to synthesize viral reverse transcriptase (See 5.3.6 and 12.1.5.). (pg. 343)

8.3.8 State that reverse transcriptase catalyzes the production of single-stranded 'novel' DNA from RNA. (These latter 2 bullets afford an opportunity to relate some aspects of DNA viral life cycle with that of the AIDS virus.)

8.3.9 Explain why reverse transcriptase is a useful tool for molecular biologists. This enzyme can make DNA from mature mRNA (such as human insulin), which can then be spliced into host DNA (Ex.- E. coli), without the introns. (pg. 374)


8.4 Translation (2 hours)

8.4.1 Outline that the structure of a tRNA allows recognition by a tRNA activating enzyme that binds a specific amino acid to it using ATP for energy. (Each amino acid has a specific tRNA activating enzyme. Degeneracy, that is, some amino acids have more than one tRNA, should also be included.) (pp. 306-307)

8.4.2 Outline the structure of ribosomes including protein and RNA composition, large and small subunits, two tRNA binding sites and mRNA binding sites. (The cloverleaf shape of tRNA and CCA at the 3' end should be included. Mention that prokaryote, chloroplast and mitochondrial ribosomes are 70s, whereas eukaryote ribosomes are 80s.)

8.4.3 State that translation consists of initiation, elongation and termination. (pp. 308-309)

8.4.4 State that translation occurs in a 5'---> 3' direction. (pg. 309)

8.4.5 Explain in detail the process of translation including GTP, ribosomes (including peptidyl transferase), polysomes, start codon and stop codons.

8.4.6 State that free ribosomes synthesize proteins for use primarily with in the cell itself and that bound ribosomes synthesize proteins primarily for secretion and lysosomes.


2.7 Genetic engineering (3 hours)

2.7.1 State that genetic material can be transferred between species because the genetic code is universal (See 2.6.6).

2.7.2 Outline a basic technique used for gene transfer involving plasmids, a host cell (bacterium, yeast or other cell), restriction enzymes (endonuclease) and DNA ligase. (pp. 364-371)

2.7.3 State 2 examples of the current uses of genetic engineering in agriculture and/or pharmacy. (pp. 378-79, 380-83)

2.7.4 Explain 1 potential harmful result of genetic engineering. (pg. 386 ?)

2.7.5 State that PCR (polymerase chain reaction) copies and amplifies minute quantities of nucleic acid. (pg. 372)

2.7.6 State that gel electrophoresis involves the separation of fragmented pieces of DNA according to their charge and size. (pg. 368)

2.7.7 State that gel electrophoresis is used in DNA profiling. (pg. 377)

2.7.8 Describe 2 applications of DNA profiling.

2.7.9 Outline the process of gene therapy using a named example.


Long & Slichter