A15_BIO_101-LCU-05_702_GenB-2

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

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 homeostasis and from an evolutionary perspective

00UV partially • To apply the experimental method in a scientific field

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

01YJ • To analyze, from an evolutionary perspective, the adaptation of multi-cellular 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

Campbell, N.A. and Reece, J.B., 2011, Biology, 9th edition, Pearson/Benjamin Cummings Publ. Co. Inc. (7th or 8th editions can be used).

* This textbook is complemented with a hard copy study guide: Taylor, M.R., 2011, Study Guide for Campbell Biology, 9th edition, Pearson/Benjamin Cummings Publ. Co. Inc.

(7th or 8th editions can be used).

Lab Manual: Marianopolis Biology Staff, Lab Manual, BIO LCU

For more information on citation styles, consult the Marianopolis Library’s citation style links at www.marianopolis.edu/resources-and-services/library/find-citation-and-research-help/

TERM: Autumn 2015 INSTRUCTOR(S): C. D’Abramo (RM I-330) S. Daly (RM I-324) C. Di Flumeri (RM B-319) U. Oberholzer (RM I-319) J. Ranger (RM I-330)

PONDERATION: 3-2-3 | Science and Liberal Arts 3-2-2 | Arts and Sciences

DISCIPLINE: Biology COURSE CREDIT: 2.66 | Science and Liberal Arts

2.33 | Arts and Sciences PREREQUISITE(S): 101-NYA-05 | Science and Liberal Arts

101-701-MS | Arts and Sciences OFFICE HOURS: Office hours will be posted on Omnivox

and your Teacher’s office door at the beginning of the term.

COURSE OUTLINE

General Biology II

http://launchpad.marianopolis.edu/wp-content/uploads/2012/09/00XU.pdf

http://launchpad.marianopolis.edu/wp-content/uploads/2012/09/00UV.pdf

http://launchpad.marianopolis.edu/wp-content/uploads/2012/09/01YJ.pdf

http://www.marianopolis.edu/resources-and-services/library/find-citation-and-research-help/

101-LCU-05 / 101-702-MS Course Outline | Autumn 2015 -

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


(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 (ΔG), 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 non- competitive 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.


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.


• 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.



• Experiments by Griffith; Avery-McCarty-MacLeod; Hershey-Chase, Meselson-Stahl; Chargaff’s rule; R. Franklin; Watson & Crick

• Structure of DNA in detail, directions of strands; antiparallel (5’3’ versus 3’5’), 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.


• 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 (5’UTR and 3’UTR)

• 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 3’UTR, 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;


3.3.4 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;

3.3.5 Understand that regulation may also take place at the post-translational level (review section on enzyme activity).


• 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.


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.

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 (5) 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.



• 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.


• 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.


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

2 CLASS TESTS First-term class test: Sept. 21 to Sept.25 Second-term class test: Oct. 26 to Oct. 30

15% 15%

22.5% 22.5%

Final exam (final exam period) 50% 35% Lab Exam: Nov. 23, 24 | lab exam [12%] + reports/quizzes [8%] 20% 20%

Total 100% 100%


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 College’s 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 person’s 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 College’s 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 else’s paper as one’s 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.

http://www.marianopolis.edu/about-marianopolis/policies/

http://www.marianopolis.edu/uploadedFiles/Content/About_Us/IPESA%20annotated%20May%206%202005.pdf

http://www.marianopolis.edu/language-policy

http://www.marianopolis.edu/student-code-of-conduct

http://www.marianopolis.edu/uploadedFiles/Content/About_Us/IPESA%20annotated%20May%206%202005.pdf


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 there-fore, 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).

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

1 Aug. 17, 18 Ped Days

2 Aug. 24, 25 Lecture and safety talk

3 Aug. 31, Sept. 1 Lab 1: Amino Acid and Protein Analysis

4 Sept. 7, 8, 10 Monday, Sept. 7 - Labour Day Tuesday, Sept. 8 - Lecture Thursday, Sept. 10 - Monday schedule, lecture

5 Sept. 14, 15 Lab 2: Protein Fractionation: GFP Purification by HIC and Protein Quantification with Biuret Reagent

6 Sept. 21, 22 Lab 3: Enzymology

7 Sept. 28, 29 Lab 4: Metabolic Pathways

8 Oct. 5, 6 Lab 5: Separation of DNA and RNA by Gel Filtration Chromatography and Gel Electrophoresis

9 Oct. 12, 13, 16 Monday, Oct. 12 - Thanksgiving Tuesday, Oct. 13 - Lecture Friday, Oct. 16 - Monday schedule, lecture

10 Oct. 19, 20 Lecture

11 Oct. 26, 27 Lab 6: DNA digestion by endonucleases

12 Nov. 2, 3, 4 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

A15_BIO_101-LCU-05_702_GenB-2

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