COURSE OUTLINE

General Biology II
TERM:
PONDERATION:
DISCIPLINE:
COURSE CREDIT:
PREREQUISITE(S):
OFFICE HOURS:

INSTRUCTOR(S): C. DAbramo (RM I-330)

S. Daly (RM I-324)
C. Di Flumeri (RM B-319)
U. Oberholzer (RM I-319)
J. Ranger (RM I-330)

Autumn 2015
3-2-3 | Science and Liberal Arts
3-2-2 | Arts and Sciences
Biology
2.66 | Science and Liberal Arts
2.33 | Arts and Sciences
101-NYA-05 | Science and Liberal Arts
101-701-MS | Arts and Sciences
Office hours will be posted on Omnivox
and your Teachers office door at the
beginning of the term.

COURSE CODE(S) AND MESRS OBJECTIVES

Science (200.B0), registered in 101-LCU-05
00XU

fully

To analyze the structure and functioning of multi-celled organisms in terms of

00UV

partially

To apply the experimental method in a scientific field

homeostasis and from an evolutionary perspective

Arts & Sciences (700.A0), registered in 101-702-MS

To analyze, from an evolutionary perspective, the adaptation of multi-cellular

01YJ

organisms to their environment

REQUIRED TEXT(S) / MATERIALS

Text Book:

Campbell, N.A. and Reece, J.B., 2012, Biology, Canadian Edition, Pearson Education Canada Inc.
(both hard copy and etext versions are available)
* This textbook is complemented with a hard copy study guide: Reece, J.B., Urry, L.A. and
Cain, M.L., 2015, Study Guide for Campbell Biology, Canadian edition.
OR
th

Campbell, N.A. and Reece, J.B., 2011, Biology, 9 edition, Pearson/Benjamin Cummings
th
th
Publ. Co. Inc. (7 or 8 editions can be used).
* This textbook is complemented with a hard copy study guide: Taylor, M.R., 2011, Study
th
Guide for Campbell Biology, 9 edition, Pearson/Benjamin Cummings Publ. Co. Inc.
th
th
(7 or 8 editions can be used).
Lab Manual: Marianopolis Biology Staff, Lab Manual, BIO LCU
For more information on citation styles, consult the Marianopolis Librarys citation style links at
www.marianopolis.edu/resources-and-services/library/find-citation-and-research-help/

4873 Westmount Ave., Westmount, Qc H3Y 1X9 Tel.: (514) 931-8792 Fax: (514) 931-8790 marianopolis.edu

COURSE CONTENT AND METHODOLOGY

General Biology II is an elective cell and molecular biology course which is required for admission to a university
program in the health sciences. It builds on the basic concepts introduced in the prerequisite course, General
Biology I, emphasizing again the relationship between structure and function, in this case at the cellular level, and
examining the regulatory mechanisms involved in homeostasis. The specific structure and function of certain
differentiated, specialized cells (nerve cells, muscle cells, cells of the immune system, etc.) is also studied. There is
a strong integrative component throughout the course, from the chemistry of macromolecules to the societal
implications of genetic engineering and recombinant DNA technology.
The targeted goals of the science program which are met by this course include:
-

to participate in labs and learn laboratory skills and techniques

to practice critical thinking
to consider the ethical questions raised by genetic engineering and gene therapy
to be able to apply the concepts learned here to new situations

1. The ponderation is 3-2-3 (3-2-2 Arts and Sciences). That is, the course material is presented in the form of
lectures (3 hours per week), and is complemented by laboratory exercises (2 hours a week). Students are
expected to spend 2 to 3 hours a week in home study and completion of lab assignments. Students are
encouraged to use MasteringBiology and the Study Guide.
2. Students can opt to do two additional assignments to meet the requirements for enriched BIO LCU (details TBA).

SPECIFIC OBJECTIVES
(Evidence of attainment of these objectives by the student.)
"Review" refers to a topic covered in General Biology.
(1)

To study the relationship between structure and function at the molecular level
1.1 Biological Macromolecules
Performance Criteria
1.1.1 Review of the chemical structure of proteins and nucleic acids (General Biology I);
1.1.2 Describe the primary, secondary, tertiary and quaternary structure of a protein, and
understand the factors which determine the 3-dimensional structure of a protein;
1.1.3 Review the structure of DNA and RNA, and understand the significance of the chemical
differences between them.

Learning objectives
Chapter 4: concept 4.3; Chapter 5: overview, concepts 5.1,5.4, and5.5
Dehydration (condensation) synthesis versus hydrolysis
Recognize structures of macromolecules (protein, DNA, RNA, based on functional groups
(phosphate, amino, carboxyl, hydroxyl, carbonyl, sulfhydryl groupspeptide and
phosphodiester bonds
functions of proteins and nucleic acids
hydrophobic, polar and charged amino acids
primary, secondary, tertiary and quaternary structures of proteins; hydrophobic, hydrogen,
ionic and covalent bonds between R groups of amino acids in a protein
effect of pH, temperature, salt concentrations and reducing agents on protein structure

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Course Outline | Autumn 2015 - Page 2

(2)

To understand the concept of energy transfer through a biological system, the metabolic pathways
involved, and the regulatory mechanisms.
2.1 Energy Transfer
Performance Criteria
2.1.1 Understand the first and second laws of thermodynamics, and apply them to a biological
system;
2.1.2 Describe a biological reaction in terms of change in free energy and entropy. Understand the
difference between a catabolic and an anabolic reaction and explain the concept of a coupled
reaction. Describe the role of ATP in energy transfer;
2.1.3 Explain the role of an enzyme in terms of the energy change in a biological reaction.

Learning objectives
Chapter 8: overview, concepts 8.1-8.3
Different forms of energy
First law: energy conservation; second law: increase in entropy and release of heat
Endergonic versus exergonic reactions in terms of change in free energy (G), anabolic/
synthesis reactions are endergonic and catabolic/breakdown reactions are exergonic
equilibrium and metabolism; disequilibrium
ATP cycle, ATP utilizing reactions (anabolic, cell movement, muscle contraction, glucose
synthesis in photosynthesis) versus reactions involved in ATP synthesis (catabolic, cellular
respiration)
Coupled reactions: ATP hydrolysis is used to drive endergonic reactions via phosphorylated
intermediate

2.2 Enzyme Chemistry

Performance Criteria
2.2.1 Understand the role of an enzyme, and the factors which determine its level of activity. Explain
the concepts of induced fit, specificity, saturation and competitive inhibition;
2.2.2 Describe the various types of co-factors and coenzymes;
2.2.3 With reference to protein structure, explain the factors which determine the level of activity of
an enzyme. Understand the concepts of allosteric change, non-competitive binding, negative
feedback effects, cooperativity.

Learning objectives
Chapter 8: concepts 8.4-8.5
specific binding of substrate to active site, induced fit, transition state, enzymes lower EA, is
reached when enzyme is saturated with substrate (substrate in excess)
energy profile of enzyme-catalyzed vs. uncatalyzed reaction
mechanisms of enzyme catalysis
cofactors (organic versus inorganic), optimal temperature and pH
enzyme regulation through molecules (regulators) activators or inhibitors that bind to
enzymes, competitive inhibition when inhibitor competes for active site versus noncompetitive inhibition when inhibitor binds to allosteric site, allosteric change of enzyme
allosteric enzymes (multiple active sites, inactive versus active forms, allosteric activators
and inhibitors (ADP versus ATP), cooperative binding of substrate)
Negative feedback (end product allosterically inhibits first enzyme of metabolic pathway)
Reversible versus irreversible inhibitions

2.3 Photosynthesis
Performance Criteria
2.3.1 Review the structure of a chloroplast;
2.3.2 Describe the light and dark reactions of photosynthesis in a eukaryote cell (C3 plant);
2.3.3 Explain the problem of photorespiration, and how it is avoided in C4 and CAM plants.

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Learning objectives
Chapter 10: overview, concepts 10.1-10.4
Photosynthesis as an overall REDOX reaction
Light dependent versus carbon fixation reactions (Calvin cycle), cellular location of these
reactions in the chloroplast
Light reactions complexes: PSII (P680), cytochrome, PSI (P700)
Properties of CHLOROPHYLL; resonance energy transfer in the light harvesting complex
(antenna) and primary electron acceptor
Concept of CHEMIOSMOSIS
Noncyclic versus cyclic electron flow: both are light-dependent reactions
Define photorespiration and when it occurs
C3, C4 and CAM plants, C4 and CAM cycles; spatial separation of C4 and Calvin cycles with
bundle sheath and mesophyll cells in C4 plants, temporal separation in CAM plants with
CAM cycle at night and Calvin cycle during day
Rubisco in the Calvin cycle versus PEP carboxylase in the C4, extra ATP needed in C4 which
comes from cyclic electron flow

2.4 Cellular Respiration

Performance Criteria
2.4.1 Review the structure of the mitochondrion;
2.4.2 Describe the steps in respiration in a eukaryote cell: glycolysis, formation of acetyl coA, Krebs
cycle, oxidative phosphorylation, chemiosmosis;
2.4.3 Apply the concept of homeostasis to explain how the rate of synthesis of ATP is regulated in
this metabolic pathway;
2.4.4 Explain how polysaccharides, lipids and proteins can be used as a source of energy in cell
respiration;
2.4.5 Describe the process of fermentation under anaerobic conditions, and compare the ATP
production under aerobic and anaerobic conditions.

Learning objectives
Chapter 9: overview, concepts 9.1-9.6

Cellular location of different steps; overall REDOX reaction

Overview of glycolysis, acetyl-CoA formation and Kreb cycle net products with 1 glucose
Drop in free energy of intermediates and final product relative to glucose
Net production of ATP during substrate level phosphorylation
Net production ATP by oxidative phosphorylation
Oxidative phosphorylation: electron transport chain (ETC), proton gradient, ATP synthase,
CHEMIOSMOSIS, apply the concepts of exergonic and endergonic to describe oxidative
phosphorylation including chemiosmosis
Comparison of oxidative phosphorylation (mito) vs. photophosphorylation (chloro)
Allosteric regulation of Phosphofructokinase (PFK) in glycolysis and homeostasis of energy
(ATP)
Alternate pathways/Versatility of Catabolism: anaerobic fermentation; hydrolysis of fats;
hydrolysis of proteins

(3)

To understand the molecular basis of the genetic continuity and information transfer in the cell, and the
mechanisms by which gene activity is regulated.
3.1 The Structure of DNA, and the Nature of the Genetic Code Intergenerational Transfer of Information
(DNA Replication)
Performance Criteria
3.1.1 Review of the chemical structure of DNA, from a historical perspective;
3.1.2 Describe the structure of chromatin in a eukaryote and compare it to the structure of a
prokaryote chromosome;
3.1.3 Describe the process of DNA replication in a eukaryote cell. Review the cell cycle and the stage
at which replication occurs;
3.1.4 Compare the process of DNA replication in a eukaryote and a prokaryote cell.

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Learning objectives
Chapter 16: overview, concepts 16.1-16.3
Experiments by Griffith; Avery-McCarty-MacLeod; Hershey-Chase, Meselson-Stahl;
Chargaffs rule; R. Franklin; Watson & Crick
Structure of DNA in detail, directions of strands; antiparallel (53 versus 35),
complementary base pairing, hydrogen bonding
Models of DNA replication: conservative, semi-conservative, dispersive
DNA replication: bidirectional, replication fork, replication bubble, identification of lagging
and leading strands given the direction of the template strands, continuous versus
discontinuous replication, Okazaki fragments
Steps in DNA replication of leading versus lagging strand; enzymes involved: DNA helicase,
Primase, single stranded DNA binding proteins, DNA polymerases, DNA ligase
Differences between eukaryotic and prokaryotic DNA replication: linear versus circular
chromosomes, multiple versus single origin of replication, end-replication problem;
telomeres ends of linear eukaryotic chromosomes, telomerase
Accuracy of DNA replication, proof-reading activity of DNA polymerase, mismatch and
nucleotide excision repair mechanisms

3.2 Information Transfer (Intra-cellular)

Performance Criteria
3.2.1 Review the chemical structure of RNA and the steps in protein synthesis. Describe the
structure of m-RNA, t-RNA and r-RNA;
3.2.2 Describe the processes of transcription and translation in a eukaryote cell. Understand the
concept of intron and exon sequences and the mechanism by which the primary transcript is
processed;
3.2.3 Describe the synthesis of a protein destined for export from the cell and explain the role of the
signal recognition particle;
3.2.4 Understand how the processes of transcription and translation differ in a prokaryote cell;
3.2.5 Understand the molecular basis of the genetic code and the various types of point mutation.

Learning objectives
Chapter 17: overview, concepts 17.1-17.6
Steps in protein synthesis common to prokaryotes and eukaryotes: Transcription initiation,
elongation and termination, RNA polymerase, transcription factors, mRNA, codons (start
and stop codons), untranslated regions (5UTR and 3UTR)
Translation initiation, elongation and termination, ribosomes (proteins and rRNA), tRNA
(anticodons, amino acid attachment site, amino acyl-tRNA synthetase), polyribosomes,
release factor, genetic code: triplet code, universal and redundant, reading frame
In eukaryotes only: recognition of promoter TATA box, mRNA processing and splicing,
ribozyme, introns, exons, cap, polyA tail, 5 and 3UTR, mRNA export
Translation and export of secreted proteins, signal peptide and signal recognition particle
(SRP)
Substitution mutations, silent, conservative (neutral), nonsense and missense mutations,
frameshift mutations by insertion or deletion of nucleotides in the coding region, effects of
mutations on amino acid sequences

3.3 Regulatory Mechanisms in Information Transfer

Performance Criteria
3.3.1 Understand the concept of positive and negative control of gene expression. Understand the
concept of constitutive and structural genes;
3.3.2 Describe the prokaryote operon in general terms. Describe the mechanisms by which an
inducible (eg lac) operon and a repressible (eg trp) operon are regulated. Explain positive
control of the lac operon through the action of CAP and c-AMP;
3.3.3 Describe the components of the promoter sequences for a eukaryote gene. Describe the role
of specific transcription factors in activation of the enhancer;
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3.3.4
3.3.5

Understand the possibility of additional control of eukaryote gene expression by one or more
of the following mechanisms: DNA methylation, histone acetylation, modulation of the rate of
transcription by cell specific transcription factors, differential processing of the primary transcript;
Understand that regulation may also take place at the post-translational level (review section
on enzyme activity).
Learning objectives
Chapter 18: overview, concepts 18.1-18.3
In prokaryotes: repressible versus inducible gene expression, generally repressible genes
encode anabolic enzymes and inducible genes encode catabolic enzymes
Operons: genetic unit consisting of single promoter controlling the expression of multiple genes
trp repressible operon for tryptophan synthesis and lac inducible operon for lactose utilization
Negative control of operon activity: trp and lac repressors, operator
Positive control of operon activity: cAMP and catabolite activator protein (CAP) in lac peron
In eukaryotes, steps regulated in gene expression: chromatin compaction, transcription
initiation, mRNA processing and splicing-alternative splicing, mRNA stability, translation
initiation, post-translational modifications protein modifications (chemical, length/
cleavage) and degradation (proteasome); role of noncoding RNAs, miRNAs
Focus on the effects of chromatin on gene expression, DNA methylation and histone
de/acetylation
Focus on the role of transcription activators (and repressors), enhancer (and silencer)
regulatory elements, co-expression of genes, cell-type specific transcription

(4)

To appreciate and understand the concept of genetic engineering, with specific reference to recombinant
DNA technology, DNA finger printing and genetic markers, gene therapy.
4.1 Bacterial and Viral Life Cycles
Performance Criteria
4.1.1 Describe the structure of a virus, and how it reproduces in the host cell. Describe the process
of reproduction in a retrovirus;
4.1.2 Compare the cycle of a lytic and a lysogenic phage;
4.1.3 Review the nucleic acid components of the bacterial cell, including plasmids. Understand the
process by which these components can be isolated;
4.1.4 List the ways in which a bacterial cell can acquire DNA: by mutation, transduction,
transformation, conjugation.

Learning objectives
Chapter 19: overview, concepts 19.1-19.3?; chapter 27, concept 27.2
General features of phages and viruses, nucleic acids packaged within capsid, membrane
envelope and glycoproteins
Types of DNA and RNA animal viruses (example of dsDNA virus: HPV); ssRNA animal viruses
(examples: Flu, HIV)
Reproductive cycle of a DNA virus, RNA virus and retrovirus-HIV, DNA/RNA replication,
transcription, reverse transcriptase, prophage, provirus, viral protein synthesis
Emerging viruses and prions
Temperate (lambda) and virulent (T4) bacteriophages, lytic and lysogenic cycles
Bacterial defenses against viruses
Describe bacterial genetics (single circular chromosomes, plasmids, binary fission),
importance of genetic variation in bacteria (especially pathogenic)
Mechanisms for producing genetic variation in bacteria: mutations; transformation;
transduction, conjugation

4.2 Recombinant DNA Technology

Performance Criteria
4.2.1 Appreciate some of the examples and applications of recombinant technology;
4.2.2 Describe the procedures involved in gene transfer from a eukaryote to a prokaryote cell, and
understand some of the problems involved.
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Learning objectives
Chapter 20: overview, concept 20.1
Cloning of DNA: make multiple copies of gene of interest to produce genetically modified
organisms (crops, animals) and to produce specific proteins for medicine
Cloning steps: bacterial plasmid, chromosomal DNA, restriction endonucleases (enzymes)
to generate sticky ends, ligation, transformation, selection for recombinant bacteria
carrying recombinant plasmid with gene-DNA of interest
Methods of selection/screening: antibiotic resistance
DNA libraries: genomic and cDNA libraries

4.3 DNA Identification and Genetic Markers

Performance Criteria
4.3.1 Describe the polymerase chain reaction and understand its significance;
4.3.2 Describe the action of a restriction endonuclease and the formation of RFLPs. Understand the
Mendelian inheritance of RFLPs;
4.3.3 Appreciate how these procedures can be used to compare DNA samples, and some of the
practical applications;
4.3.4 Understand how these procedures can be used to develop genetic markers for heritable
diseases, using sickle cell anemia as an example;
4.3.5 Explain how the base sequence of a DNA sample can be determined.

Learning objectives
Chapter 20: parts of concepts 20.1-20.2
Describe the procedures of polymerase chain reaction (PCR), restriction fragment length
polymorphisms (RFLPs), DNA gel electrophoresis to detect RFLPs and their use in forensics,
paternity testing or detection of inherited diseases

4.4 Gene Therapy

Performance Criteria
4.4.1 Integrate what has been learned with respect to recombinant DNA technology and viruses,
and describe and evaluate current gene therapy procedures.

(5)

Learning objectives
Chapter 20: concept 20.4
Replace a defective gene with a functional one in specific cells of the body (stem cells)
Treatment of severe combined immunodeficiency (SCID) using a recombinant retroviral
vector to transduct human cells

To apply the concept of homeostasis at the organismal level through the study of signal transduction in
specialized systems.
5.1 Defense Mechanisms
Performance Criteria
5.1.1 List the types of white blood cells;
5.1.2 Describe non-specific defense mechanisms and the inflammatory response. Describe the role
of cytokines;
5.1.3 Describe the chemical structure of an immunoglobin, and the nature of an antigen-antibody
reaction. Describe the effects of antibody production, and the action of complement;
5.1.4 Explain the sequence of events which results in the production of antibodies in the humoral
immune response;
5.1.5 Explain the difference between active and passive immunity, with examples;
5.1.6 Describe the cell mediated immune response, and the role of cytokines;
5.1.7 Understand some of the problems associated with impaired immune function: Explain how an
HIV infection can result in an immunodeficiency. Understand the role of the histocompatibility
complex, types I and II. Explain the nature of an autoimmune disease and give examples.
Explain what an allergic reaction is.

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Learning objectives
Chapter 43: overview, concepts 43.1-43.4
Location of immune cells: bone marrow, blood, lymphatic system, spleen, thymus and skin
Defense mechanisms: Innate (nonspecific) versus acquired/adaptive (specific)
Innate: external defenses (skin, mucous membranes and secretions) versus internal
defenses (phagocytic cells-neutrophils, macrophages, natural killer cells, antimicrobial
proteins like interferons and complement proteins, and inflammatory response)
Acquired/adaptive: humoral and cell-mediated responses; helper T-cells play a central role
in both responses
Humoral response: antigen presenting cells (dendritic cells, macrophages); activation of
helper T- lymphocytes; clonal selection of B lymphocytes (memory and plasma); production
of immunoglobulins/antibodies in response to antigens
Interaction between helper T- and B-cells: chemical interactions between T-cell receptor
and major histocompatibility complex type II (MHCII) of B-cell; release of cytokines
Role of antibodies: recognize specific epitopes (antigen surfaces); antigen disposal by
neutralization, opsonization or activation of complement system and pore formation
Primary and secondary responses; active (vaccination ) versus passive (antibodies from
another immunized person) immunization
Cell-mediated response: cytotoxic T-lymphocytes, perforin and granzymes, killing of
infected cells, interaction between cytotoxic T and infected cells requires MHC type I and
release of cytokines
Disorders of the immune system: allergies; autoimmune diseases; immunodeficiency

5.2 Nerve Cell Function

Performance Criteria
5.2.1 Describe the structure of a neuron;
5.2.2 Explain the basis of the resting membrane potential;
5.2.3 Describe the changes in membrane potential which occur when a nerve is stimulated. Describe
the properties of a nerve impulse (action potential) and relate these properties to the
membrane changes described;
5.2.4 Describe transmission of the nerve impulse across a chemical synapse and a gap junction.

Learning objectives
Chapter 48: overview, concepts 48.1-48.4
Neuron, dendrites, cell body, axon hillock, axon, axon terminals, sensory neuron,
interneuron, motor neuron
Resting potential; -70mV, negative inside; Na+/K+ pump, resting channels (passive)
Action potential (AP): stimulation to threshold, depolarization, Na+ influx through Na+
voltage channels (gated), repolarization and hyperpolarization, K+ efflux through K+ voltage
channels (gated), undershoot/refractory period
Propagation of AP
Synaptic transmission: presynaptic versus postsynaptic cells/neurons, Ca2+ voltage
channels, synaptic vesicles, neurotransmitters, release in synapse, postsynaptic receptor
channels, inhibitory versus excitatory neurotransmitters and effect on cell body of
postsynaptic neuron, summation of inhibitory postsynaptic potentials IPSP and excitatory
postsynaptic potentials EPSP

5.3 Muscle Contraction

Performance Criteria
5.3.1 Describe the microscopic structure of a striated muscle cell, and the sarcomere unit. Relate the
microscopic structure to the arrangement of actin and myosin filaments;
5.3.2 Describe the molecular structure of the actin and myosin filaments;
5.3.3 Trace the sequence of events from the arrival of a nerve impulse at the motor end plate to the
contraction of the muscle, followed by relaxation. Explain the role of ATP, and the source of
ATP.
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Learning objectives
Chapter 50: concept 50.5
Skeletal muscle, muscle fiber, myofibrils, sarcomeres (repeating units)
Sarcomeres: Actin thin filaments; Myosin thick filaments
Activation of muscle contraction: neuromuscular junction, presynaptic motor neuron,
postsynaptic muscle fiber, release of neurotransmitter (acetylcholine), generation of AP,
release of calcium from sarcoplasmic reticulum
Interaction of actin and myosin filaments: calcium binds to troponin, displacement of
tropomyosin away from myosin binding sites on actin subunits, power-stroke/sliding
filament model
Power-stroke: using ATP hydrolysis to pull/slide actin filaments inwards relative to myosin,
shortening of sarcomeres, muscle contraction and relaxation
Energy for muscle contraction: ATP (immediate source)

5.4 The response of a target cell to a hormone/signal transduction

Performance criteria
5.4.1 Describe signal transduction and the 3 stages involved;
5.4.2 Describe the reception, transduction and responses in the case of a steroid hormone;
5.4.3 Describe the reception, transduction and responses of a target cell to a peptide/protein or
amine hormone. Understand the concept of second messengers. Understand the concept of a
cascade reaction (amplification) and the role of a protein kinase.
Learning Objectives
Chapter 11: concepts 11.1-11.4
Provide examples of signal transduction functions and describe the 3 stages involved:
reception, transduction and response
Distinguish cytoplasmic and intracellular receptors and describe the three types of
cytoplasmic receptors: G protein coupled receptors, receptor tyrosine kinases and ion
channel receptors
Describe different types of transduction pathways: phosphorylation cascades and
pathways mediated by second messengers such as cAMP, inositol triphosphate (IP3)
and/or ions (Ca2+)
Describe different types of responses: cytoplasmic versus nuclear responses providing
examples for each
Describe different types of inactivation and their functions.

EVALUATION
The evaluation policy in this course is in accord with those policies specified in IPESA, Institutional Policy on
Evaluation of Student Achievement.
1.

The student will demonstrate his/her knowledge of class material by writing two class tests during regular
lecture periods, and a final examination in the final exam period.

2.

To demonstrate his/her understanding of lab material, the student will write one lab exam. This will be in two
parts comprising stations and a theoretical section. A student who has not attended labs cannot take the lab
exam. Failure of the lab exam does not result in an automatic failure in the course.
The marking scheme which is most advantageous
to the student will be used.

Marking
Scheme #1

Marking
Scheme #2

15%
15%
50%
20%
100%

22.5%
22.5%
35%
20%
100%

2 CLASS TESTS
First-term class test: Sept. 21 to Sept.25
Second-term class test: Oct. 26 to Oct. 30
Final exam (final exam period)
Lab Exam: Nov. 23, 24 | lab exam [12%] + reports/quizzes [8%]
Total
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Students should be familiar with the terms of the Institutional Policy on Evaluation of Student Achievement (IPESA).
Evaluation of students work will reflect the performance criteria listed above under the objectives of the course as
well as the criteria of the ministerial English Exit Exam, as noted in the Marianopolis Language Policy: comprehension
and insight, organization of response, and expression. In particular, students must make a conscious effort to express
themselves clearly and coherently in all of their work.
For further information about evaluation, please consult the Institutional Policy for the Evaluation of Student
Achievement (IPESA) and the Language Policy available at www.marianopolis.edu/about-marianopolis/policies/

ENRICHMENT COMPONENT: See Course Content and Methodology - page 2, point 2.

POLICIES OF MARIANOPOLIS COLLEGE
Institutional Policy on the Evaluation of Student Achievement (IPESA)
The Institutional Policy on the Evaluation of Student Achievement (IPESA) reflects the Colleges philosophy on
education and guides the assessment of student achievement by way of progressive and systematic evaluation.
This policy describes the goals and objectives of such evaluation, documents the means taken to arrive at
comprehensive and fair evaluation, and establishes the rights and sharing of responsibilities for all participants. All
students and faculty, administration and staff members are responsible for knowing the provisions of the policy.
The Marianopolis IPESA is available online: www.marianopolis.edu/ipesa
Language Policy
The Marianopolis graduate shall be prepared to bring the powers of thought and language not only to the
challenge of academic studies but also to that of personal and public leadership in the contemporary world. In all
course activities, attention shall be paid to the structure of thought and the language characteristic of the
discipline; to reinforcing and integrating the language objectives of the different programs; and to the criteria of
the ministerial exit examination in language: comprehension and insight, organization of response, and expression.
High standards in the quality of written and spoken language shall be maintained. The Marianopolis Language
Policy is available online: www.marianopolis.edu/language-policy
Student Code of Conduct
This document outlines expectations for Student behaviour.
The Marianopolis Student Code of Conduct is available in your Student Agenda and online:
www.marianopolis.edu/student-code-of-conduct
Academic Integrity
In keeping with the principles of fairness and honesty and consistent with the standards upheld by institutions of
higher learning, the College is committed to promoting and protecting academic integrity. Students are expected to
properly acknowledge any other persons contribution to their work, when such contributions are permitted, in
conformity with the guidelines provided by the teacher.
Cheating is a serious academic offence. Cheating means any dishonest or deceptive practice. It includes, but is not
restricted to, making use or being in possession of unauthorized material, obtaining or providing unauthorized
assistance for any submitted work, false claims about the submission of work, disobeying the Colleges Examination
Rules, plagiarism, or attempting to do any of the above.
Plagiarism occurs when a student presents or submits the work of another, in whole or in part, as his or her own. It
includes but is not limited to using material or ideas from any source that is not cited, submitting someone elses paper
as ones own, receiving assistance from tutors, family, or friends that calls the originality of the work into question.
Suspected instances of cheating and plagiarism will be reported to the Associate Academic Dean and the
Department Chair. The penalty shall be decided by the Associate Academic Dean, and may include, but is not limited
to, a grade of zero on the plagiarized work; a grade of zero in the course; and/or expulsion from the College. Any
judgment resulting in this grade or penalty is final; associated work is excluded from any grade appeal, and no
assignment may replace such work.
Regulations related to cheating and plagiarism are available online in the Marianopolis IPESA:
www.marianopolis.edu/ipesa Section 4, page 14.
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POLICIES SPECIFIC TO THIS COURSE

General Policies Regarding the Lab
In order to fulfill targeted goals of the science program, this course includes mandatory participation in
labs and learning of laboratory skills and techniques. It is therefore compulsory that students attend all
labs and arrive on time at all labs in order to obtain passing grade in the course.
Absence for medical reasons requires a note from a physician. If you know in advance that you must miss
a lab and you have presented a valid excuse to your teacher, then you may ask the technician if it is
possible to take the lab in another section for that week. Absence without a valid excuse means you will
not be fulfilling the targeted program goal mentioned above, therefore, marks will be deducted.
If you arrive late, you will be missing instructions that include issues of procedure and safety, and therefore, you will not be meeting the targeted goals mentioned above. If this occurs without a valid medical or
urgent personal reason, marks will be deducted.

Rules for testing situations

In order to ensure that no student has an unfair advantage over the other students, the only calculator
permitted during quizzes, class tests and final examinations at the College is Texas Instruments
Model TI-30XII (B or S).

101-LCU-05 / 101-702-MS

Course Outline | Autumn 2015 - Page 11

MARIANOPOLIS COLLEGE
AUTUMN 2015
GENERAL BIOLOGY II LAB SCHEDULE
101-LCU-05/ 101-702-MS
Lab Technician: Alexandra Adam and Renu Chitra

Monday, Tuesday Schedule

WEEK

DATES

BIO LCU LAB ACTIVITY

Aug. 17, 18

Ped Days

Aug. 24, 25

Lecture and safety talk

Aug. 31, Sept. 1

Sept. 7, 8, 10

Sept. 14, 15

Lab 1: Amino Acid and Protein Analysis

Monday, Sept. 7 - Labour Day
Tuesday, Sept. 8 - Lecture
Thursday, Sept. 10 - Monday schedule, lecture
Lab 2: Protein Fractionation: GFP Purification by HIC and
Protein Quantification with Biuret Reagent

Sept. 21, 22

Lab 3: Enzymology

Sept. 28, 29

Oct. 5, 6

Oct. 12, 13, 16

Lab 4: Metabolic Pathways

Lab 5: Separation of DNA and RNA by Gel Filtration
Chromatography and Gel Electrophoresis
Monday, Oct. 12 - Thanksgiving
Tuesday, Oct. 13 - Lecture
Friday, Oct. 16 - Monday schedule, lecture

10

Oct. 19, 20

Lecture

11

Oct. 26, 27

12

Nov. 2, 3, 4

Lab 6: DNA digestion by endonucleases

Monday, Nov. 2 - Holiday
Tuesday, Nov. 3 - Lecture
Wednesday, Nov. 4 - Monday schedule, lecture

13

Nov. 9, 10

Lab 7: Purification of Plasmid DNA and Lac Operon Genetics

14

Nov. 16, 17

Lab 8: Transformation of E. coli with pGlo

15

Nov. 23, 24

Lab Exam

16

Dec. 1, 2

Review