Learning Objectives
Learning Objectives
Learning Objectives
Continue to the next page for Learning Objectives for each topic.
Note: There are four Units in the course, and each module inside the unit is
numbered, e.g. for Unit 1, there is Unit 1-1, 1-2, below.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
Prior knowledge:
▪ List and evaluate the characteristics that define cells as the smallest unit of life.
▪ Compare and contrast the structural properties of bacterial and eukaryotic cells
Targeted:
▪ Identify the four phases of population growth in a batch culture and in the
associated growth curve graph - lag phase, exponential (log) phase, stationary
phase, and death phase.
Prior knowledge:
▪ Identify how the highly electronegative atoms (for example O and N) lead to uneven
electron sharing and permanent dipoles when bonded to other biologically relevant
atoms.
▪ Predict the types of non-covalent interactions that can form between functional
groups within a molecule or between molecules.
Prior knowledge:
Targeted:
▪ Refer to Chemistry for Biology Learning objectives, which will be featured throughout
the course.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
Targeted:
▪ Predict which structures (micelles or bilayers) will form when different kinds of lipids
are mixed with water .
▪ Describe how the cell membrane is both a container and a barrier using the Fluid
Mosaic model of biological membranes.
Prior knowledge:
Targeted:
▪ Predict the permeability of various types of molecules across lipid bilayers based
on size and charge.
▪ Predict the type of transport occurring based on the transport graph data.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
Targeted:
▪ Draw the generic structure of an amino acid and identify the key functional groups.
▪ Identify a peptide bond between amino acyl residues in a polypeptide (i.e. be able
to circle it on a structure).
▪ Predict the likely R-group properties of amino acids based on their location within a
protein’s folded structure (i.e. interior vs. exterior)
▪ Predict the effects of changing amino acids on protein structure and function.
▪ Describe the spontaneous assembly and folding of proteins using the relative
terms; stability, bond strength, spontaneous and entropy (i.e. the hydrophobic
effect).
Targeted:
▪ Describe and recognize the structural components of nucleic acids, including the
monomers, the directionality, and the reason for the directionality.
▪ Describe the key features of the DNA double helix, such as the sugars,
phosphodiester bonds, bases; base pairs; base pair geometry; the major/minor
grooves.
▪ Identify the non-covalent interactions that determine DNA structure, such as base
stacking and H-bonds.
▪ Explain how the entropy of water drives the hydrophobic effect with respect to DNA.
▪ Label a schematic diagram of double stranded DNA to show the 3’ and 5’ ends,
including the functional group found at each 3’ and 5’ position.
Targeted:
▪ Describe the biological information flow from DNA to proteins in cells, and the role
of transcription and translation in this process.
▪ Describe the role of messenger RNA molecules as a link between genes and
proteins.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
Targeted:
▪ Draw the structure of transcription units (a gene) in both bacteria and eukaryotes,
clearly differentiating between regulatory and transcribed regions.
▪ Explain and Identify upstream and downstream regions of the genome when used
to describe relative location of gene structures.
▪ Explain the difference between the template strand and the non-template (coding)
strand in DNA.
▪ Compare and contrast the structure of the transcription units in bacteria and
eukaryotes.
Targeted:
▪ Explain how the interaction of a transcription factor and the promoter of a gene
leads to repression or the initiation of transcription.
▪ Predict the RNA sequence transcribed from the DNA sequence of a transcription
unit.
▪ Predict the types of non-covalent interactions likely to form between DNA and a
protein involved in transcription.
▪ List the various eukaryotic mRNA processing events – 5’-capping, splicing, and
poly-adenylation (polyA tails).
▪ Explain how RNA splicing can be used to produce different mature mRNA
transcripts/proteins from the same pre-mRNA and determine the correct splicing
pattern for any mature mRNA.
▪ Compare and contrast the structures and functions of the different types of RNA
molecules: rRNA, tRNA, mRNA.
Unit 2-5: Translation-RNA to protein
Targeted:
▪ List RNAs involved in the process of translation and describe their roles.
▪ Explain the function of aminoacyl tRNA synthetase enzymes and why they are
described as “the translators” of the genetic information.
▪ Describe the roles of the ribosome binding sites (RBS) in bacteria and eukaryotes,
the start codon, and stop codons on a mRNA.
▪ Predict the anticodon of a tRNA for a given amino acid using the codon table.
Prior Knowledge:
▪ Explain the terms genotype and phenotype.
▪ Compare the definitions of genome, chromosome and gene in terms of the DNA in
the cell.
Targeted:
▪ Identify the three different types of point mutations (when one base in the DNA is
changed): missense, nonsense, and silent mutations.
▪ Predict the effects of a point mutation in the coding region of the gene on the
resulting amino acid sequence and analyze how/if this will change the protein
structure/function.
▪ Explain the roles of guide RNA, Cas9, and target DNA in CRISPR/Cas9 genome
editing.
Unit 2-7: Regulation of Gene Expression
▪ Explain how the presence of a nutrient results in the induction of the operon
encoding the genes to digest that nutrient.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
▪ Identify the structural components of a bacterial operon and define the roles of each
component in operon regulation.
▪ Explain the logic of the function and regulation of an operon relative to the
availability of a food source (for example, lactose or maltose).
▪ Draw a correct representation of an operon that includes the structural genes in the
operon, the promoter and operator regions, as well as the regulatory gene with its
product and promoter.
▪ Predict the binding of positive or negative regulator proteins to the operator region
of an operon based on the presence and absence of the signal molecule.
▪ Explain how the presence of a signal molecule results in the induction of an operon
that is positively regulated.
▪ Predict what happens to transcription, if there are mutations in the DNA sequences
of either the gene encoding the regulator protein or the operon elements (operator,
promoter, genes, etc.).
▪ Apply the principles of gene expression learned from lac or mal operon to explain
other examples of transcriptional regulation.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
▪ Compare and contrast DNA replication in vitro (PCR) and in vivo (in cells).
▪ Place DNA replication within the growth phases for bacterial or eukaryotic cells (i.e.
lag, log/exponential, stationery and death phase).
▪ Explain the logistics of the DNA replication process including how the cell solves the
problems of:
o Separating the DNA strand.
o Synthesizing primers and providing primers for the leading and the lagging
strands during replication (DNA synthesis).
o Distinguish between and label the leading and the lagging strands of DNA in
a replication fork.
▪ Predict the types of non-covalent interactions that enable interactions between DNA
and DNA-binding proteins.
Unit 3-2: DNA replication in vitro – Polymerase chain reaction (PCR)
▪ Explain why PCR is such an important technique in molecular biology (i.e. why do
we care about making lots of copies of a specific piece of DNA) and identify practical
uses of PCR.
▪ Describe the three key steps in polymerase chain reactions; denaturation, annealing
and extension, and explain what role these play in the replication of DNA in a test
tube.
▪ List the components needed (in a test tube) to start a PCR amplification experiment.
▪ Identify the structural “end” of a DNA molecule where dNTPs are added during DNA
synthesis.
▪ Predict what primers would be needed to amplify a given piece of double stranded
DNA.
Unit 4- Metabolism
Big picture learning objective for Unit 4:
▪ Recognize the ubiquity of central metabolic pathways across the tree of life.
▪ Compare (remembering the first law of thermodynamics) and contrast (using the
vocabulary of oxidation and reduction) the functions of mitochondria and
chloroplasts.
▪ Identify the functional inputs and outputs for each of the metabolic processes (and
any combination of these) and how they contribute to cellular metabolism:
o Glycolysis
o Fermentation
o Pyruvate processing and the Citric Acid Cycle
o Oxidative Phosphorylation
o Photophosphorylation
o The Calvin Cycle
Prior Knowledge:
▪ Explain the role of the enthalpic (ΔH) and entropic (ΔS) factors in the Gibbs Free
Energy (ΔG) equation.
Copyright: BIOL 112: Biology of the Cell, University of British Columbia - Modified Jan 3, 2024
Targeted:
▪ Describe the types of nutrients required for metabolic function for the cell.
▪ Explain how the high energy phosphate bonds of ATP make it a good energy
carrier, for example, in anabolic polymerization reactions of a nucleic acid strand.
▪ Define and identify redox reactions using examples of organic compounds and high
energy electron carriers.
▪ Identify reduced and oxidized states of organic molecules and high energy electron
carriers.
Unit 4-3: Glycolysis and Fermentation
▪ Describe the function of NADH produced and predict the fate of the NADH that is
produced during glycolysis.
▪ Discuss the role of fermentation and how end products such as lactate and ethanol
play a role in NAD+ regeneration.
▪ Evaluate the redox state of C atoms in glucose, fermentation end products such as
lactate, and CO2 and use this to explain the relative amounts of ATP generated by
fermentation and respiration.
Note: the citric acid cycle is also called the Krebs or tricarboxylic acid (TCA) cycle.
▪ Contrast the cellular locations of acetyl-coA synthesis and the citric acid cycle in
bacterial and eukaryotic cells.
▪ Identify the inputs and the outputs of acetyl-coA synthesis and the citric acid cycle.
▪ Identify when ATP synthesis by substrate level phosphorylation (SLP) occurs during
cellular respiration (this will include glycolysis) or citric acid cycle.
▪ Describe the role of the electron carriers such as NADH and FADH2 in metabolism.
▪ Describe the general process of electron transport and how it creates the proton
gradient in the ETC.
▪ Explain the chemiosmotic theory and how the ETC drives ATP synthesis using a
proton gradient.
▪ Predict and describe how metabolic inhibitors such as dinitrophenol (DNP) can
alter the function of the ETC.
Unit 4-6: Photosynthesis – Photophosphorylation and the Calvin Cycle
Targeted:
▪ Explain the source of electrons and role of light in generating the proton gradient in
chloroplasts and other oxygenic phototrophs (cyanobacteria).