Cayon, St. Kitts, West Indies.
====================================================
Spring 2016 Semester
BCHM 550: Medical Biochemistry and Genetics
1. WELCOME
The Medical Biochemistry and Genetics faculty welcomes you to the Biochemistry
module during which will help you understand the normal cellular processes that sustain
life and the molecular basis of many diseases. This syllabus has been developed to give the
student a detailed idea about the course teaching, learning, and assessment methods.
1. a. Course Description
Medical Biochemistry and Genetics course is designed to prepare the student for
understanding the basic cellular mechanisms that enable us to survive. Biochemistry is the
chemistry of life. The major objective of this module is to enable students understand the
molecular level of all of the chemical processes in living cells and their abnormalities. All
disease has some biochemical basis. A sound knowledge in Biochemistry is essential for
other disciplines like Physiology, Pharmacology and Microbiology .Most of the recent
advances in modern medicine have been possible with the insight into the molecular basis
of the diseases. Genetics deals with the molecular structure and function of genes, patterns
of inheritance from parent to offspring, and gene distribution, variation and change in
populations and changes in gene expression in various normal and disease states. A basic
knowledge in genetics is essential for all students of medicine.
In addition to lectures, students will participate in Small group sessions, PBL sessions,
Student Seminars and Self Study assignments.
Student assessment will use both formative and summative methods and students will be
provided timely feedback about their performance throughout the course
1
1. b. General objective of the course:
The objectives and content of the Medical Biochemistry and Genetics course are designed
to provide students with a comprehensive understanding of cellular structure and function,
and the manner by which cellular processes are normally integrated and regulated. This
course stresses both the normal cellular function, and why disease states occur if normal
cellular processes are disrupted.
The course also stresses on understanding and discussing the basic principles of heredity
and describing the clinical features and the genetic transmission of diseases.
We shall encourage students to understand the molecular basis of health and disease
and apply biochemical principles in clinical practice.
1. b. i . Specific objectives of the course:
At the end of the course students will be able to
 Describe the process by which Biomolecules are synthesized and function.
 Describe the manner in which biological energy is stored, retrieved and generated.
 Integrate intersecting pathways of metabolism within a variety of tissues,
emphasizing the functional significance and regulatory mechanisms that permit
homeostasis
 Describe causes of disease on a molecular and genetic level.
 In preparation for medical practice, develop awareness of the role of molecular
biology as a tool used in biomarker development, diagnostics, prognostics,
pharmacological development and intervention.
 Develop knowledge of basic principles of medical genetics and apply them to
understanding of the etiology, diagnosis, progression, and treatment of genetic
disease.
2
2. Instructors:
Dr. Guri Tzivion, PhD,
Professor of Genetics, Molecular Biology and Immunology,
Department Chair
Email: tzivion@windsor.edu
Dr. Soumitra Chakravarty MBBS, MD (Biochemistry),
Associate Professor of Biochemistry
Course Director
Email: soumitra@windsor.edu
Dr. Vivek Joshi MBBS, MD (Biochemistry)
Associate Professor of Biochemistry
Email: vivek@windsor.edu
2. a. Office hours:Dr.S.Chakravarty: Monday & Wednesday 10:00 AM to12:00 PM.
Dr. Tzivion Guri: Monday: 9AM-5PM & Wed-Fri: 9AM-11PM
Dr. V. Joshi: Monday & Wednesday 10:00 AM to12:00 PM.
The student can visit at any specific time by earlier appointment irrespective of office
hours and can visit immediately in case of any emergency!
3. Application of the course objectives to Clinical practice:
In collaboration with other basic science subjects and ICM students will learn to apply
scientific principles to diagnosis, management and prevention of diseases.
Students will demonstrate clinical competence with special emphasis of rational drug
therapy.
Students will be able to understand and respond to important social factors which influence
the use of medicine including pharmaceutical promotion.
Students will be able to communicate and predict disease producing conditions in an
effective and compassionate manner to a simulated patient.
Will be able to critically appraise the prescribing of self and colleagues and medicine use in
health facilities using objective criteria
3
Will be able to use objective, unbiased sources of medical information and be able to obtain
up-to-date information about current and new laboratory investigations and new molecular
aspects of disease mechanisms.
Educational
Biochemistry and
objectives of the
medical genetics
School
learning objective
1.Patient care
 To be able to
 Obtain a
diagnose
sufficient level
various
of medical
diseases from
knowledge to
information
understand the
provided in
basic facts,
form of a
concepts, and
principles
clinical case
essential to
sign/symptom
competent
s or various
medical
laboratory
practice.
tests and
 Exhibit the
analysis.
highest level of
effective and
efficient
 To be able to
performance in
recall the
data gathering,
normal
organization,
interpretation
reference
and clinical
ranges of the
decision making
biochemistry
in the
analytes,
prevention,
hormones
diagnosis, and
especially in
management of
disease.
critical
emergency
situations
Learning methods Assessment
methods
 Interactive
lectures
 Small group
sessions
 Integrated
PBL
 Self-study
assignments
 MCQs
 Formative
assessment
during PBL
sessions
 Assessment
during PBL
presentation
s
 Evaluation
of submitted
assignment
 Structured
viva voce
 Formative
assessment
during small
group
sessions
4
 To be able to
understand the
expected
changes in the
same in any
abnormalities
of metabolic
pathways.
 To predict and
understand the
metabolic
changes that
can occur with
use of
therapeutic
drugs.
2.Medical Knowledge
 Apply scientific
principles and a
multidisciplinar
y body of
scientific
knowledge to
the diagnosis,
management,
and prevention
of clinical
problems.
 Describe the
basic
metabolic
pathways and
the disorders
of the same.
 Understanding
the molecular
basis of the
diseases.
 Describe the
types of
genetic
transmission
of diseases.
 Interactive
lectures
 Small group
sessions
 Integrated
PBL
 Self-study
assignments
 MCQs
 Formative
assessment
during PBL
sessions
 Assessment
during PBL
presentation
s
 Evaluation
of submitted
assignment
 Structured
viva voce
 Formative
assessment
during small
5
group
sessions
3.Interpersonal and
Communication skills
 Demonstrate
effective and
compassionate
interpersonal
communication
skill toward
patients and
families
necessary to
form and sustain
effective
medical care.
 Present
information and
ideas in an
organized and
clear manner to
educate or
inform patients,
families,
colleagues and
community.
4.Professionalism
Display the personal
attributes of
compassion, honesty
and integrity in
relationship with
patients, families, and
the medical
community.
 Counsel a
simulated
patient
regarding
many issues
like role of
diet, lifestyle,
substance
abuse etc. in
health and
diseases.
 Interactive
lectures
 Small group
sessions
 Integrated
PBL
 Self-study
assignments
 Review of
medical
literature
sessions
 To be able to
counsel a
simulated
patient
effectively on
antenatal
screening and
issues related
 Small group
sessions
 Formative
Assessment
during
Student
Seminars
 Structured
viva voce
 Formative
assessment
during small
group
sessions
 OSCE
 Structured
viva voce
 Formative
assessment
during small
group
sessions
6
 Practical
examination
to neonatal
screening.
 Understandin
g the impact
of unethical
marketing
strategies
taken by
suppliers of
diagnostic
tests kits and
equipment
and their
impact on the
patients.
5.Practice based
learning
improvement
 Understand the
limits of personal
knowledge and
experience and will
demonstrate the
intellectual
curiosity to actively
pursue the
acquisition of new
knowledge and
skills necessary to
refine and improve
his/her medical
practice or to
contribute to the
scientific body of
medical
knowledge.
 Evaluating
new
information
about
metabolic
processes and
disease
processes.
 Using
independent,
objective
sources of
information to
obtain up to
date
information
about
 CME
 Critical
review of
scientific
literature on
recent
advances in
etiology,
diagnosis,
therapy and
prognosis of
various
disorders.
 Attending
conferences
for attaining
knowledge
 Credits and
certificates
from CMEs,
conferences,
seminars
and research
publications.
7
metabolic
disorders.
 Understanding
the impact of
unethical
marketing
strategies
taken by
suppliers of
diagnostic
tests kits and
equipment and
their impact
on the
patients.
regarding
the same
 Conducting
active
research for
advancemen
t of
medicine
and medical
education.
4. ORGANIZATION OF THE COURSE.
Syllabus for medical Biochemistry and Genetics (with specific learning objectives)
The Medical Biochemistry and Genetics syllabus mainly comprises of the following
topics:4. a. BIOCHEMISTRY
Introduction to Biochemistry
Biological oxidation
At the end of this lecture, the student must be able to:
 List the enzymes involved in substrate level phosphorylation in Glycolysis and TCA
cycle
8
 Name the Mobile and fixed Complexes involved in electron transport chain
 Describe the Chemiosmotic theory and proton motive force of electron transport
chain
 Calculate the number of ATP generated by NADH and FADH2
 Describe the poisons that inhibit complex 1 and 4 of electron transport chain
 List the Function of Uncouplers, Oligomycin and Atractyloside in inhibiting ETC
Carbohydrate chemistry:
At the end of this lecture, the student must be able to:
 Classify carbohydrates based on four different properties
 List the various clinical uses of carbohydrates
 Describe the clinical uses of various polysaccharides
 Differentiate Glycosaminoglycans and Glycoproteins and its clinical implications
 Explain Mucopolysaccharidoses and I-cell disease
 Describe some of the Lysosomal storage diseases and their clnical significance
Citric acid cycle:
At the end of this lecture, the student must be able to:
 List the cofactors required for Pyruvate dehydrogenase complex
 Explain the regulation of pyruvate dehydrogenase enzyme
 State the causes of congenital and acquired lactic acidosis
 Describe the citric acid cycle in detail and its intermediates involved in synthesis of
various amino-acids and vice versa
 Explain how Citrate regulates TCA cycle and fatty acid synthesis in an opposite way
 Calculate the energy yield of TCA cycle and its regulation
 Describe the Shuttle mechanisms required for transport of NADH into mitochondria
Glycolysis:
At the end of this lecture, the student must be able to:
 Analyze the importance of Glycolytic pathway that it can produce ATPs in both
aerobic and anaerobic environment
 Differentiate between substrate level and oxidative phosphorylation
 List the GLUT transporters and classify them based on insulin dependency
 List the rate limiting and irreversible steps of Glycolysis and their regulation
 Explain the Importance of Embden-Meyerhof pathway
 Describe the clinical features of pyruvate kinase deficiency
 Calculate the Energy generated during aerobic and anaerobic Glycolysis
9
Glycogen metabolism:
At the end of this lecture, the student must be able to:
 Describe the enzymes involved in Glycogenesis and Glycogenolysis
 State the rate limiting steps in Glycogenesis and Glycogenolysis
 List the ways of activation and regulation of Glycogenolysis in muscle
 Differentiate the clinical features of various Glycogen storage diseases and mention
their enzyme deficiencies
HMP pathway:
At the end of this lecture, the student must be able to:
 Describe the important steps in the HMP pathway and its importance
 List the byproducts of HMP pathway and its uses
 List the uses of NADPH in various biological reactions
 Briefly describe the role of glutathione and NADPH in maintaining the integrity of
RBC membranes
 Describe G-6PD deficiency and its clinical presentation
Gluconeogenesis:
At the end of this lecture, the student must be able to:
 List the various substrates used for Gluconeogenesis
 List the 4 key steps of gluconeogenesis
 Briefly describe the regulation of gluconeogenesis by glucocorticoids
 Describe the role of Acetyl co-A as an positive allosteric regulator for pyruvate
carboxylase and as a negative allosteric regulator for pyruvate dehydrogenase
 Explain the Importance of Glucose-Alanine and Cori cycle
Metabolism of Galactose and Fructose:
At the end of this lecture, the student must be able to:
 List the key enzymes of Galactose and Fructose metabolism
 Differentiate the clinical features and the enzyme deficiency in essential Fructosuria
and hereditary fructose intolerance
 Differentiate the clinical features and enzyme deficiency in non-classical and
classical Galactosemia
 Briefly describe lactose intolerance and its clinical manifestations
 Describe the pathogenesis of Diabetes Mellitus and its complications
Overview of carbohydrate metabolism and general concepts
At the end of this session students should be able to:
10
 Describe the basic regulatory mechanisms in maintaining blood glucose
concentration.
 Describe the metabolic adaptations in fasting and fed state.
 Describe the interrelationships and integration between various metabolic pathways
in the body.
Chemistry of Lipids
At the end of this session students should be able to:
 Classify lipids and fatty acids based on their structure
 Describe the functions of lipids
 List the various lipases acting on triglycerides in different parts of the body
 List the components of Phospholipids and Glycolipids
 Describe the properties of Omega 3 and omega 6 fatty acids
 Describe the Functions of phospholipase A2 and C
 Classify the types of Phospholipids and Glycolipids
 Analyze the Composition of surfactant and its importance
 Describe the Sphingolipid metabolism and the enzyme deficient in various
sphingolipidoses
Biosynthesis of fatty acids
At the end of this lecture the students will be able to : List the sources of NADPH required for fatty acid synthesis
 List the key enzymes of fatty acid synthesis
 Describe the role of citrate in bringing acetyl Co-A to cytosol for FA
synthesis
 Explain the regulation of acetyl Co-A carboxylase.
 Explain the functions of adipose tissue in the body
 Explain the importance of glycerol kinase in the liver.
11
Beta -oxidation of fatty acids and ketogenesis
At the end of this lecture students will be able to : Describe the role of carnitine in fatty acid transport across mitochondria
for oxidation and list the fatty acids which do not require carnitine for
transport.
 Describe the functions of Carnitine and its deficiency due to primary and
secondary causes.
 Differentiate the clinical features of CPT-1 and CPT-2 deficiency
 Differentiate the various types of oxidation of fatty acids and its
importance
 Describe the clinical features of MCAD deficiency and its treatment
 Describe Zellweger syndrome and Jamaican vomiting sickness
Lipid transport and storage
At the end of this lecture a student will be able to –
 Describe the composition of various lipoproteins and list the key Apo proteins
 Describe the various pathways of lipoprotein metabolism in detail
 List the enzymes and receptors involved in lipoprotein metabolism and their
deficiency states
 Classify Lipoproteinemias and describe the clinical features of various
lipoproteinemias
 Describe the pathogenesis of atherosclerosis
 List the drugs used to treat hyperlipoproteinemias and its mechanism of action
Biosynthesis of cholesterol & Bile acid metabolism
At the end of this session a student will be able to : List the important steps in synthesis of cholesterol and its rate limiting step
 List the products derived from cholesterol as a substrate
 Describe the mechanism of action of statins on HMG-coA reductase and its side
effects
 Describe the regulation of HMG-coA reductase in detail
 Differentiate primary and secondary bile salts, its formation, secretion and
enterohepatic circulation
 Explain the importance of conjugation of bile salts and list the drugs interfering with
bile acid metabolism
12
Globular proteins :Hemoglobin and Myoglobin
At the end of this session students should be able to:
 Describe the properties of globular proteins
 Describe the structure and function of haemoglobin and myoglobin
 Analyse the oxygen dissociation curve and factors affecting oxygen dissociation
curve
 Differentiate the features of fetal and adult haemoglobin
 List the various physiological and pathological modifications of haemoglobin
 List the steps in treatment of cyanide poisoning
 Describe the formation of Glycated haemoglobin and its use in monitoring diabetes
Heme synthesis and porphyrias
At the end of this session students should be able to:
 Describe the steps in Heme synthesis pathway and outline the important enzymes
regulating the pathway
 List the defects in the Heme synthetic pathway and its clinical implications
 Differentiate the clinical features of Hepatic and Erythropoeitic porphyria
 List the enzymes inhibited by lead poisoning and explain Sideroblastic anemia
 Analyze the steps in diagnosis of various types of porphyrias and its treatment
Heme degradation and Jaundice
At the end of this lecture, the student must be able to:
 Explain the steps in breakdown of Heme in the reticuloendothelial cells
 Describe the steps in conjugation of Bilirubin in the liver and excretion into bile
 List the causes for congenital and acquired Hyperbilirubinemias
 Differentiate the features of Unconjugated and conjugated Hyperbilirubinemias
 List the Blood parameters used to diagnose Hyperbilirubinemias
 List the Changes in urine parameters in various Hyperbilirubinemias.
Hemoglobinopathies
At the end of this lecture, the student must be able to:
 List the sites of haemoglobin synthesis in various stages of development of fetus to
adult
 Mention the Chromosomes involved in Globin chain synthesis
 Classify Hemoglobinopathies based on qualitative and quantitative defects in
Globing synthesis
 Describe the genetic defect, clinical features, complications and treatment of sickle
cell anemia
13
 Classify Thalassemia. Describe the genetic defect, clinical features, complications
and treatment of alpha and beta thallasemias
Urea cycle and its defects
At the end of this lecture, the student must be able to:
 Explain the fate of carbon skeleton and nitrogen group of amino acids
 Explain the ways of transport of nitrogen from various parts of the body to the liver
 Describe the urea cycle and the enzymes involved in production of urea in the liver
 Define and classify Hyperammonemias. List the enzymes deficient in various
hyperammonemias and its clinical features
Aromatic aminoacid metabolism:
At the end of this lecture, the student must be able to:
 Explain the steps in synthesis of various non-essential fatty acids in the body
 List the molecules derived from aromatic amino acids and their uses
 Discuss the enzyme deficiencies of aromatic amino acid metabolism and their
clinical features
 Differentiate various types of phenylketonuria and its diagnosis
 Discuss the clinical features of Alkaptonuria and its treatment
Sulphur containing and basic amino acid metabolism
At the end of this lecture, the student must be able to:
 Discuss the molecules derived from tryptophan and its biological functions
 Describe the steps in Tryptophan metabolism and the enzymes deficiency states
 Describe the steps in synthesis of Niacin and the cofactors required
 Describe the diseases associated with tryptophan metabolism
 Discuss the metabolism of sulphur containing amino acids. Classify
homocysteinuria and its clinical manifestations
 Discuss the metabolism of basic amino acids and their defects.
Branched chain amino acid metabolism and Glycine:
At the end of this lecture, the student must be able to:
 Discuss the steps in branched chain amino acid metabolism
 Classify organic acidurias and differentiate their clinical features
 Discuss the formation , metabolic fate and important products formed from Glycine
Acid base balance and metabolic implications
At the end of this lecture the student must be able to :
 Describe the various mechanisms that work to counteract the changes in body pH
14
 Identify the various acid base disorders especially in an ICU setting.
 Analyze arterial blood gas data to diagnose a particular acid-base disorder
 Identify the compensatory mechanisms that try to restore the body pH to normal
Nucleotide metabolism
At the end of this lecture, the student must be able to:
 Discuss the components of Nucleotides and molecules contributing to formation of
purine and pyrimidine ring
 Describe the Pyrimidine metabolism and its defects – Orotic acidurias and
Megaloblastic anemias
 Differentiate the features of Denovo and salvage pathways of purine metabolism
 List the causes of Hyperuricemias, its clinical features and treatment
 Discuss the clinical features and the enzyme defects in SCID and Lesch - Nyhan
syndrome – clinical features
 List the anticancer drugs acting on purine and pyrimidine metabolism and its
mechanism of action
Vitamins
At the end of this lecture, the student must be able to:
 Classify vitamins based on the physical and chemical properties
 Discuss the General properties of vitamins
 Differentiate between fat and water soluble vitamins
 Enlist the Functions of individual vitamins
 Discuss the Vitamin deficiencies and its clinical manifestations
 Explain the steps in diagnoses of various vitamin deficiencies
Mechanism of Hormone action , Cell signaling and Signal Transduction
At the end of this lecture, the student must be able to:
 List the various types of receptors in the cells
 Differentiate the features of water and fat soluble hormones
 List the various second messengers involved in signal transduction
 Describe the G protein and its coupled receptor in detail
 Differentiate intrinsic and extrinsic tyrosine kinase mediated pathways of signal
transduction
 Describe the mechanism of insulin release and the structure of insulin receptor
4.b. MOLECULAR BIOLOGY
15
Components of Molecular biology:
At the end of this lecture, the student must be able to
 Define the central dogma of molecular biology
 Describe the basic components of nucleotides and its nomenclature
 Define Chargaff Rule and apply it in calculating the percentage of nucleotides in an
unknown sample of DNA or RNA
 Outline the features of Watson and crick model of DNA
 List the various types of RNA and its functions and compare each RNA
 Describe the special features and modifications of each subtype of RNA
 Describe the functions of nucleolus and P-bodies
 Describe the Structure and components of Ribosome – and differences between
prokaryotic and eukaryotic ribosome
DNA organization:
At the end of this lecture, the student must be able to:
 Outline the properties and functions of Histone proteins
 Describe the packing of DNA into higher order structure – chromosomes
 Describe the principle of karyotyping and its interpretation
 List the parts of a Chromosome and outline the principles of banding techniques
 Differentiate Coding and non-coding regions of DNA
 Compare the functions of Introns and Exons
DNA replication:
At the end of this lecture, the student must be able to:
 Differentiate between prokaryotic and eukaryotic replication
 List the various Steps of DNA replication
 Differentiate between prokaryotic and eukaryotic polymerase and its proof reading
activity
 Outline the functions of various enzymes of replication
DNA repair and cell cycle regulation:
At the end of this lecture, the student must be able to
 Outline the Causes and Types of DNA damage that can occur in the living cell
 Describe in detail the 4 types of DNA repair mechanisms
 List the Key enzymes associated with DNA damage repair mechanisms and their
defects
 Briefly describe the stages of cell cycle and its check points
 Explain the importance of P53 and Rb proteins in cell cycle regulation
Transcription:
16
At the end of this lecture, the student must be able to:
 List the types of RNA, its structure and functions
 Classify the types of RNA polymerases and its functions
 Outline the steps of RNA transcription and its clinical applications
 Processing of RNA in the nucleus and P-bodies
 Differentiate between prokaryotic and eukaryotic ribosomes and its RNA
 List the Drugs acting on transcription
Translation:
At the end of this lecture, the student must be able to:
 Explain the principles of genetic code
 Application of Wobble hypothesis for relaxation of 3rd nucleotide in the genetic
code
 Outline the steps of translation – initiation, elongation and termination
 Describe the regulation of translation
 List the drugs that inhibit various stages of protein synthesis
Gene regulation:
At the end of this lecture, the student must be able to:
 Describe the Lac operon in E.coli and its application in various
 Define operon and cistron. Differentiate monocistronic and polycistronic mRNA
 Explain Histone acetylation and DNA methylation
 Describe the Concept of Epigenetics
 Discuss the Mechanism of alternative splicing
 Mention the role of Transcription factors in Gene regulation
 Discuss the Higher order elements like enhancers and repressors and their role in
regulation of gene expression
Molecular Biology techniques and Recombinant DNA technology
• Describe the Concept of cloning and its applications
• List the steps in PCR and its clinical applications
• Explain the Principles of RFLP
• Discuss the Concept of Gene therapy and its clinical applications
• Explain the principles of Gel electrophoresis and its clinical applications
• Discuss the various types of blotting techniques and enlist the uses
17
4.c. MEDICAL GENETICS
Mendelian genetics:
At the end of this lecture, the student must be able to:
 Explain the Mendelian laws and its application in various clinical conditions
 Describe the Dominant and Recessive genes in Autosomal and x-linked inheritance
patterns in various single gene disorders
 List the special features of Autosomal dominant inheritance
 Analyze the pattern of mitochondrial inheritance and compare it autosomal and xlinked inheritance
 Describe the Punnet squares and calculate the risk in various generations
Population Genetics :At the end of this lecture, the student must be able to:
 Describe genotype , phenotype and allele frequency
 Understand penetrance and solve problems based on this principle
 Apply Hardy Weinberg’s law to solve questions based on Population genetics
Cytogenetics:- At the end of this lecture, the student must be able to:
 Recognize the chromosomes in human karyotyping
 Describe euploidy, polyploidy, aneuploidy and understand their causes.
 Describe reciprocal and Robertsonian translocation
 Understand the causes and describe the causes of the following syndromes :
- Down syndrome
- Turner Syndrome
- Edward Syndrome
- Patau Syndrome
- Cri-du-Chat syndrome
 Describe the formation of ring chromosome and isochromosome
 Describe FISH and Spectral Karyotyping
Genetic disorders:
At the end of this lecture, the student must be able to:
 Describe the Non disjunction of chromosomes during mitosis and meiosis and their
effects
 Differentiate Robertsonian and reciprocal translocations
 List the examples of Autosomal and sex chromosomal non disjunctions
 Explain the Trinucleotide expansion and its associated clinical conditions
 Explain Genomic imprinting and its effects
A. List the various small and large scale genetic mutations
18
Genetic Testing
At the end of this lecture, the student must be able to:
 Explain the use of RFLP analysis to solve problems on genetic disorders
 Describe DNA fingerprinting and foot-printing
Remaining lectures :-Revision Classes in Biochemistry and Genetics
4. d. INTEGRATION WITH OTHER COURSES
The Medical Biochemistry and Genetics course will integrate horizontally
with anatomy, physiology and vertically with neurosciences, pharmacology,
pathology and microbiology.
5. SELF STUDY ASSIGNMENT
Student Assignments
Assignments have to handwritten and in the student’s own language as far as
possible.
At present the department is planning to use self-study assignments in one topic:
“1) Role of Vitamins in metabolism
There shall be integrated assignments for students involving other subjects as
well.
6. INTEGRATED PBL SESSIONS
(To be introduced very soon)
These sessions will be conducted in an integrated manner with Physiology,
Anatomy, Neurosciences and Epidemiology.
Students will be assessed using their participation in small group work and
presentations.
7. SMALL GROUP SESSIONS
These sessions aim to equip students with the skills required to use both clinical
knowledge and use Laboratory evidence. In the present session we plan to have
ten sessions which will address the topics mentioned below:
1. Small group discussion
19
Clinical case discussion and analysis sessions –Clinical case study
sessions with in-depth analysis of approximately 40 clinical cases.
For details please refer to Schedule of classes.
 Students will work in small groups supported by different resources and a faculty
member of Biochemistry and Genetics will act as a facilitator. Students will present
their findings in a plenary session and the facilitator will add his inputs.
Students will be assessed based on their performance and involvement
in small group work and their performance by a practical examination at the
conclusion of the session.
8. TEXTBOOKS
8. a. TEXTBOOKS FOR BIOCHEMISTRY
1. Champe PC, Harvey R and Ferrier D. Lippincott’s Illustrated Reviews: Biochemistry.
5th Edition, 2010. Lippincott Williams and Wilkins, Philadelphia. (ISBN: 9781608314126)
This is a very easy to read book with very good diagrams and illustrations .The
chapters that deal with molecular biology are very nicely written.
2. Harper’s illustrated Biochemistry. 29th edition, McGraw-Hill Medical; (ISBN- 9780071765763)
This text book is a highly recommended book to read for the metabolic pathways of
carbohydrates, lipids, proteins, nucleotides and the integration of metabolic
pathways.
8. b. TEXTBOOKS FOR GENETICS
1.
Textbook: Human Genetics and Genomics, 4th edition, Bruce R. Korf & Mira B.
Irons, publisher: Wiley-Blackwell.
20
2.
3.
4.
5.
Concepts of Genetics, 10th edition, William S. Klug, Michael R. Cummings and
Charlotte Spencer, publisher: Benjamin Cummings.
Genetics in Medicine 6th edition, Robert L. Nussbaum
Medical Genetics for the Modern Clinician, Judith A. Westman
Biochemistry, Molecular Biology & Genetics, Michael A. Lieberman
8. c. ADDITIONAL TEXTBOOKS AND E-RESOURCES
1. Swanson TA, Kim SI and Glucksman MJ. BRS Biochemistry, Molecular Biology,
and Genetics, 5th Edition. Lippincott Williams & Wilkin. (December 7, 2009).
(ISBN:978-0781798754)
2. Dudek RW. High Yield Cell and Molecular Biology. Lippincott Williams &
Wilkin.(ISBN: 978-0781768870)
3. Marks Basic Biochemistry, a clinical approach. 4th edition. Michael Lieberman, PhD;
Allan D. Marks, MD. ISBN: 978-1-60831-572-7
4. Kaplan resources – www.kaptest.com
5. USMLE world resources -www.uworld.com
6. Ebsco : https://search.ebscohost.com
User id: wusm2012
Password: Please ask the librarian.
9. EXAMINATIONS AND GRADING:
9. a. Assessment and examinations:






Formative Quizzes
MCQs during lectures
Performance during small group sessions and seminars
Block 1 exam (Summative)
Block 2 exam (Summative)
NBME exam (Summative)
9. b. WEIGHTAGE OF BLOCK EXAMS AND NBME EXAM ON FINAL GRADE
21





Block 1 exam (Summative)-30%
Block 2 exam (Summative)-30%
NBME exam (Summative)-30%
Lab and internal assessment - 10%
Total - 100%
Important: Absolute standard for Passing is 65%
9. c. GRADING SYSTEM
GRADES
A/H (Honors)
B / HP(High Pass)
C/P (Pass )
D/SP (Pass )
F - FAIL
PERCENTAGE
90–100%
80-89%
70-79%
65-69%
< 65%
The minimum passing grade for courses offered in the School of Medicine is D or Pass or
a minimum of 65%.
Absence in any exam is considered as a FAIL grade for the same exam. Students absent in
any exam can appeal to the Promotion’s Committee if the student has a genuine reason for
being absent. (Refer to section 3.1.1 of the Promotion’s policy)
10. INSTRUMENTS USED FOR STUDENT ASSESSMENTS
10. a. Student presentation evaluation checklist
Name: _____________________________________________________
Topic: _____________________________________________________
Date: ____________
Evaluation criteria
Poor 1
Satisfactory 2
Good 3
Excellent 4
Total
( Please tick )
Appearance & body
language
Clarification of objectives
Interest & enthusiasm
Audiovisual aids
22
Organization of
presentation
Voice (clarity,
modulation)
Sticking to time
Summarizing
Answering questions
Sources for further
reading
TOTAL OUT OF 40
Positive points about the presentation:
Areas where the presenter can improve:
11. ATTENDANCE POLICY:
1. Attendance at classes held on/off campus and all small group sessions are mandatory.
2. Students are encouraged to attend all of their classes. Attendance records are kept by
the School and are released to licensing authorities or government bodies if requested.
It is mandatory that an attendance level of at least 80% is maintained as some states
may request this information prior to offering a licence.
3. If the student’s attendance falls below 80% they will not be allowed to sit for the final
examination and will have to appeal to the Dean of Students Affairs and Promotions
committee. Also there is a fine that has to be paid even if promotions committee
decides to allow to sit for final exams.
4. Attendance is expected for the whole period of class. Students must make sure they
are present at the commencement of class and remain until the class is concluded.
11. a. WITHDRAWING from the course: Students may voluntarily withdraw from the
course at any time.
Please see materials in the STUDENT HANDBOOK promulgated by WUSM for details.
23
12. STUDENT MISCONDUCT: See the STUDENT HANDBOOK for WUSM policies.
Its policies shall be strictly enforced.
13. Learning methods in Biochemistry and Genetics:
1. Interactive lectures hours 120 hours
2. Small group practical learning sessions with Clinical case discussion 17 hours
3. Self-directed learning 15 hours
14. GENERAL SCHEDULE OF LECTURES
Please refer to the weekly schedule on our Learning management system
‘moodle.windsor.edu’ for weekly schedules
BIOCHEMISTRY
MOLECULAR BIOLOGY AND GENETICS
Day
Topics
Topics
Mon
Orientation day
Orientation day
Tue
Introduction to Biochemistry and Genetics
Introduction to Genetics and Molecular Biology 1
Wed
Enzymes 1
Introduction to Genetics and Molecular Biology 2
Thu
Enzymes 2
Fri
Biological oxidation and electron transport
chain 1
Mon
Biological oxidation and electron transport
chain 2
Chemistry of carbohydrates 1
Tue
Genes, Chromosomes and Heredity 1: from Mendelian to modern genetics
Genes, Chromosomes and Heredity 2: Cell Cycle, Mitosis and Meiosis
24
Wed
Genes, Chromosomes and Heredity 3: Chromosome Organization
Thu
Chemistry of Carbohydrates &
mucopolysaccharidoses
TCA cycle
Fri
___________________________
DNA: Structure, Replication and Regulation of Gene Expression 1:
The genetic code, replication, recombination and transcription
Mon
Glycolysis
Tue
Glycogen metabolism 1
Wed
Glycogen metabolism 2
Thu
Gluconeogenesis 1
Fri
___________________________
Mon
QUIZ 1
Tue
Gluconeogenesis 2
Wed
Thu
Metabolism of monosaccharides - Fructose ,
Galactose and Uronic acid pathway
HMP shunt 1
Fri
___________________________
Mon
HMP shunt 2
Tue
Regulation of blood sugar levels
Basics of Molecular Biology 3: Human genome project
Wed
Hemoglobin chemistry 1
Genetics of Organisms and Populations 1: Quantitative genetics and
multifactorial traits
Thu
REVIEW LECTURE
Fri
_________BLOCK EXAM
____________________
Mon
Hemoglobin chemistry 2
Tue
Hemoglobinopathies 1
QUIZ 2
Wed
Hemoglobinopathies 2
Inherited genetic diseases 1: Simple genetic diseases 1
Thu
REVIEW LECTURE
Fri
___________________________
Mon
Biosynthesis of heme 1
Tue
Biosynthesis of heme 2 (Porphyrias)
Inherited genetic diseases 2: Polygenic diseases 1
Wed
Heme catabolism 1
Inherited genetic diseases 2: Polygenic diseases 2
Thu
Heme catabolism 2 - Jaundice and Liver
function tests
DNA: Structure, Replication and Regulation of Gene Expression 2:
Translation and proteins
DNA: Structure, Replication and Regulation of Gene Expression 3:
Gene mutations and DNA repair
DNA: Structure, Replication and Regulation of Gene Expression 4:
Regulation of gene expression
Basics of Molecular Biology 1: Recombinant DNA technologies,
genetic engineering and proteomics 1
Basics of Molecular Biology 1: Recombinant DNA technologies,
genetic engineering and proteomics 2
Basics of Molecular Biology 2: Transgenic animals, gene therapy and
cloning
Genetics of Organisms and Populations 2: Population genetics
Inherited genetic diseases 1: Simple genetic diseases 2
25
Fri
________________________
Inherited genetic diseases 1: Cancer 1
Mon
Chemistry of Lipids1
Tue
Chemistry of Lipids 2- Sphingolipidoses
Biosynthesis of fatty acids and TG synthesis
Wed
Biosynthesis of fatty acids and TG synthesis
Inherited genetic diseases 3: Cancer 2
Thu
Beta oxidation of fatty acids 1
Fri
_____________________________
Mon
Beta oxidation of fatty acids 2 -ketogenesis
Tue
Lipid transport - lipoprotein metabolism 1
Lipid transport - lipoprotein metabolism 2
Wed
Biosynthesis of cholesterol 1
Molecular Therapeutics 1: Genetic screening, SNP’s and
high-throughput sequencing 2
Thu
Fri
Biosynthesis of cholesterol and bile acid
metabolism 2
________________________________
Mon
Amino acid chemistry 1
Tue
Structural Organization of Proteins
Structural proteins : Collagen , Elastin and Biosynthesis of collagen
Wed
Defects of structural proteins 1
Molecular Therapeutics 2: Cancer classification and personalized medicine 2
Fri
________________________________
Molecular Therapeutics 3: Drug development and pharmacogenetics 1
Mon
QUIZ 3
Tue
Defects of structural proteins 2
Protein catabolism 1
Wed
Thu
Protein catabolism 2 - defects of Urea cycle
metabolism of aromatic amino acids 1
Molecular Therapeutics 3: Drug development and pharmacogenetics 2
Fri
__________________________________
USMLE Step 1 and NBME question samples and review 1
Mon
metabolism of aromatic amino acids 2
Tue
metabolism of sulfur containing amino acids 1
metabolism of sulfur containing amino acids 2
Wed
USMLE Step 1 and NBME question samples and review 2
Thu
metabolism of simple and branched chain
amino acids
Nucleotide metabolism
Fri
_______________________________________
USMLE Step 1 and NBME question samples and review 3
Mon
Tue
Signal transduction and Mechanism of hormone
action
Fat soluble vitamins
Block Exam
Wed
Nutrition
USMLE Step 1 and NBME question samples and review 4
Thu
REVIEW
Fri
_______________________________________
Molecular Therapeutics 1: Genetic screening, SNP’s and
high-throughput sequencing 1
Molecular Therapeutics 2: Cancer classification and personalized medicine 1
Thu
USMLE Step 1 and NBME question samples and review 5
26
Wishing you success and good luck with the Medical Biochemistry and
Genetics course at Windsor University School of Medicine!
27